WO2024133323A1 - Hydrolysed protein dispersants - Google Patents

Abstract

The present invention relates to dispersants for suspension type water medium agrochemical formulations, where said formulations comprise at least one dispersant being a hydrolysed vegetable protein having molecular weight of at least 5,000 Da; and at least one agrochemical active. Preferably, the hydrolysed protein is derived from potato, wheat, or chickpea protein. The hydrolysed protein may be chemically modified with a functional group selected from silicones, or alkenyl succinic anhydride. The hydrolysed protein may be crosslinked with di- or tri- glycidyl ethers which are optionally alkoxylated. There is also a method of providing dispersancy in said agrochemical formulations using said hydrolysed protein, and methods of treating crops with such formulations. A concentrate is also provided suitable for forming the formulation.

Description

Hydrolysed protein dispersants

The present invention relates to dispersants for suspension-type agrochemical formulations with hydrophobic solid agrochemical actives, and a method of providing dispersancy in said agrochemical formulations. The present invention also includes methods of treating crops with such formulations.

Agrochemical formulations typically include dissolved or dispersed components such as actives and additives or dispersants are often added to formulations to help disperse these components.

Regulations are driving a trend to more water based systems which causes problems for actives which are not very water soluble (hydrophobic sparingly soluble). Additionally often when more active is included in a formulation this can lead to unfavourable crystal growth. A particular problem with agrochemical formulations is there is an increasing difficulty in dispersing actives, and this is especially an issue due to the trend for using less or sparingly soluble actives.

Recently, there is also a desire to remove fossil-fuel based ingredients from agrochemical formulations, and instead provide more sustainable alternatives to traditional dispersants.

Therefore, there is a need to find dispersants which allow for formation of suspension type with hydrophobic sparingly soluble actives, and overcome the above described problems. Additionally, the present invention seeks to provide dispersants which have desired properties such as dispersancy of hydrophobic solid actives in suspension type formulations, and are from more sustainable sources. The present invention also seeks to provide the use of agrochemical concentrates and dilute formulations comprising said dispersants.

According to a first aspect of the present invention there is provided a suspension type water medium agrochemical formulation comprising; i) a hydrolysed vegetable protein dispersant, said protein having molecular weight of at least 5,000 Da; and ii) at least one solid agrochemical active dispersed in aid water medium.

According to a second aspect of the present invention there is provided a concentrate formulation suitable for making an agrochemical formulation of the first aspect, said concentrate comprising; i) a hydrolysed vegetable protein dispersant, said protein having molecular weight of at least 5,000 Da; and ii) at least one solid agrochemical active dispersed in aid water medium.

According to a third aspect of the present invention there is provided the use of a hydrolysed protein in accordance with the first aspect, as a dispersant in an agrochemical formulation comprising solid agrochemical active.

According to a fourth aspect of the present invention there is provided a method of treating vegetation to control pests, the method comprising applying a formulation of the first aspect, and/or a diluted concentrate formulation of the second aspect, either to said vegetation or to the immediate environment of said vegetation.

It has been found that a hydrolysed protein, provide for desired dispersancy properties when used in a suspension type agrochemical formulation having at hydrophobic solid agrochemical active. Additionally, the hydrolysed protein is obtainable from non fossil-fuel sustainable sources.

As used herein, the terms ‘for example,’ ‘for instance,’ ‘such as,’ or ‘including’ are meant to introduce examples that further clarify more general subject matter. Unless otherwise specified, these examples are provided only as an aid for understanding the applications illustrated in the present disclosure, and are not meant to be limiting in any fashion. It will be understood that, when describing the number of carbon atoms in a substituent group (e.g. ‘Ci to Ce alkyl’), the number refers to the total number of carbon atoms present in the substituent group, including any present in any branched groups. Additionally, when describing the number of carbon atoms in, for example fatty acids, this refers to the total number of carbon atoms including the one at the carboxylic acid, and any present in any branch groups.

The term ‘hydrolysed protein’ is used herein to mean proteins which have been subject to hydrolysis. The hydrolysed protein may comprise protein fragments, polypeptides, peptides, amino acids and/or peptones.

The term ‘hydrolysed protein’ is used herein to include polypeptides, peptides, amino acids and/or peptones. Polypeptides, peptides and amino acids may, for example, be produced by acid, alkali and/or enzyme hydrolysis, of native proteins. Alkali hydrolysed proteins are preferred. In one embodiment, hydrolysed potato proteins are preferred, in particular produced by alkali hydrolysis. The hydrolysed protein component may also contain carbohydrates, for example hydrolysed potato protein may contain potato starch.

The hydrolysed protein may be produced by acid hydrolysis, alkali hydrolysis, and/or enzyme hydrolysis of, preferably, naturally occurring proteins or proteins from renewable sources. Without being bound by theory, an advantage of alkali hydrolysis when compared with acid or enzyme hydrolysis is that the alkali hydrolysis producing higher molecular weight soluble hydrolysed proteins, when compared with acid or enzyme hydrolysis. In general, acid hydrolysis may produce the smallest fragments by weight average molecular weight, alkali hydrolysis may produce the largest fragments, while enzyme hydrolysis may produce fragments of intermediate size between acid and alkali hydrolysis.

The size of a fragment in the hydrolysed protein is proportional to the number of amino acid residues in the fragment since the fragments come from the long amino acid chains which make up the un-hydrolysed protein. Alkali hydrolysis may be advantageous in order to obtain hydrolysed proteins of the desired molecular weights.

The amino compound used in making the composition of the invention may be a partially hydrolysed protein. The term ‘partially hydrolysed protein’ means a protein that has not been hydrolysed completely i.e. not been hydrolysed to the extent that only individual amino acids remain in the amino compound.

The amino compound used in making the composition of the invention may be a chemically unmodified hydrolysed protein. The term ‘chemically unmodified hydrolysed protein’ means a protein that has not been further chemically modified (or reacted) other than by hydrolysis.

Preferably the composition does not comprise a protein component obtained from an animal protein source. This is advantageous since animal sources can be undesirable for consumers. Preferably the composition comprises no animal derived components. Preferably the composition is suitable for vegan consumers.

The hydrolysed protein present use in the present invention is derived from vegetable sources, or by fermentation. Preferably from vegetable sources. Examples of suitable proteins include collagen, chickpea, hemp, elastin, keratin, casein, wheat protein, wheat starch, potato protein, soya protein and/or silk protein. Particularly preferred are potato protein, hemp protein, and chickpea protein. Especially preferred is potato protein.

The hydrolysed protein may be formed from individual amino acids, or from amino acids comprised within longer peptide chains that are derived from hydrolysed protein. Preferably the hydrolysed protein may be amino acids chain formed from hydrolysing a protein.

The dispersant may be partially hydrolysed protein, preferably obtained from a potato source, wheat source, or chickpea source. The potato, wheat, or chickpea protein source may be a potato, wheat, or chickpea protein concentrate and/or isolate. An aqueous dispersion of the potato, wheat, or chickpea protein concentrate and/or isolate may be made as a first step and the protein may be hydrolysed as a second step. A difference between the potato, wheat, or chickpea protein source and the partially hydrolysed protein may be that the partially hydrolysed protein is more soluble in water at a reference temperature (e.g. room temperature) than the potato, wheat, or chickpea protein source.

The partially hydrolysed protein may be produced by acid, alkali or enzyme hydrolysis. Alkali hydrolysis is preferred. One or more enzymes may be used. Preferably the enzyme is from a micro-organism source. The enzyme(s) may comprise a carbohydrase and/or a protease. The hydrolysis may be performed to the extent required to achieve the desired weight average molecular weight of the hydrolysed protein. The extent of hydrolysis may be varied by varying the temperature, acid / alkali / enzyme used, and time taken. The resulting hydrolysed protein may be filtered and/or treated to remove undesired material. For example the hydrolysed protein may be treated to remove any chloride ions present if acid hydrolysis is used.

The molecular weight (weight average) of the protein component starting material (prior to hydrolysis) may vary over a wide range.

The weight average molecular weight (Mw) of the hydrolysed potato, wheat, or chickpea protein may be at least 5,000 Daltons (Da), preferably at least 8,000 Da, more preferably at least 10,000 Da, particularly at least 15,000 Da. The weight average molecular weight may be at most 180,000 Da, preferably at most 160,000 Da, more preferably at most 140,000 Da, particularly at most 130,000 Da, especially at most 110,000 Da.

Where the hydrolysed protein comprises crosslinking, the molecular weight or the hydrolysed protein prior to crosslinking may be lower. The lowest range of the weight average molecular weight (Mw) of the hydrolysed potato, wheat, or chickpea protein may be at least 3,000 Daltons (Da), preferably at least 4,000 Da.

The molecular weight will be determined by size exclusion chromatography such as size-exclusion HPLC (SE-HPLC) as described herein, specifically the TSKgel GMPWXL Protocol.

The hydrolysis performed will be to the extent required to achieve the desired molecular weight and chain length of the hydrolysed protein. The hydrolysed protein may be filtered and treated to remove undesired material.

It is preferred that the hydrolysed protein component is capable of forming a solution in water.

Preferably, the amount of free amino acid in the hydrolysed protein is less than 60 wt.%. More preferably less than 55 wt.%. It will be understood that as the free amino acid has low solubility it is desired that the amount is at a low level.

The dispersant may be partially hydrolysed protein obtained from a hemp source. The hemp protein source may be a hemp protein concentrate and/or isolate. An aqueous dispersion of the hemp protein concentrate and/or isolate may be made as a first step and the protein may be hydrolysed as a second step. A difference between the hemp protein source and the partially hydrolysed protein may be that the partially hydrolysed protein is more soluble in water at a reference temperature (e.g. room temperature) than the hemp protein source.

The partially hydrolysed protein may be produced by acid, alkali or enzyme hydrolysis. Alkali hydrolysis is preferred. The hydrolysis may be performed to the extent required to achieve the desired weight average molecular weight of the hydrolysed protein. The extent of hydrolysis may be varied by varying the temperature, acid / alkali / enzyme used, and time taken. The resulting hydrolysed protein may be filtered and/or treated to remove undesired material. For example, the hydrolysed protein may be membrane washed to remove any salt present.

The molecular weight (weight average) of the hydrolysed hemp protein may vary over a wide range, such as for example in the range from 1,000 Da to 500,000 Da, preferably 5,000 Da to 200,000 Da, more preferably 10,000 Da to 150,000 Da. In one embodiment, the hydrolysed protein may have an average molecular weight in the range from 15,000 Da to 100,000 Da, preferably 20,000 Da to 80,000 Da, in particular 25,000 Da to 75,000 Da, for example about 70,000 Da.

The molecular weight will be determined by size exclusion chromatography such as size-exclusion HPLC (SE-HPLC) as described herein.

The hydrolysed protein may be copolymerised with a hydrophilic polymer. In particular, the hydrophilic polymer may be selected from polyvinylpyrrolidone (PVP), polyvinyl alcohols, polyvinyl alcohol copolymers, polyglycol alkylacrylates, polyethers, polyether alkyl methacrylates, polyvinyl acetates, and polyvinyl acetate copolymers. Preferably the hydrophilic polymer is selected from polyvinylpyrrolidone, polyethers, polyether alkyl methacrylates, and poly glycol alkylacrylates.

More preferably, suitable hydrophilic polymers may be selected from polyvinylpyrrolidone, poly vinyl alcohols, poly glycol methacrylate (HEMA), and poly (ethylene glycol) methyl ether methacrylate (PEGMA). Most preferably, the hydrophilic polymer is polyvinylpyrrolidone.

The protein-hydrophilic polymer copolymer used in the present invention is suitably produced by reacting protein with hydrophilic polymer, preferably by a free radical polymerisation process known in the art.

The ratio of hydrophilic polymer to protein to reacted together to form the protein- hydrophilic polymer copolymer (or ratio of hydrophilic polymer to protein present in the copolymer) is suitably in the range from 2 to 98:2 to 98%, preferably 5 to 70:30 to 95%, more preferably 10 to 50:50 to 90%, particularly 15 to 40:60 to 85%, and especially 20 to 25:75 to 80% by weight.

The resulting copolymer may be of any suitable type, including liner copolymers such as block, or branched copolymers such as graft or star. Branched copolymers may be preferred. In particular, graft copolymers may be particularly preferred.

The hydrophilic polymer used herein suitably has a molecular weight (weight average) in the range from 1,000 to 40,000, preferably 5,000 to 20,000.

Hydrolysed chickpea protein may be preferred when copolymerised with PVP and chemically modified with octenyl succinic anhydride (around 24 wt.%).

The molecular weight (weight average) of the polymeric binders described herein can is determined by HPLC (SE-HPLC) as described herein, specifically the TSKgel GMPWXL Protocol.

Where present, the hydrophilic polymer may represent from 10 to 50 wt.% of the total copolymerisation reagents. Preferably, from 13 wt.% to 35 wt.% of the reagents. More preferably, from 15 wt.% to 30 wt.%.

Chemically modified proteins and/or hydrolysed proteins may also be employed, for example where the protein has been covalently reacted with a functional group, e.g. silicones, or alkenyl succinic anhydride. The or each hydrolysed protein may independently be further chemically modified, for example where the protein has been covalently reacted with said functional group.

One or more of the hydrolysed proteins may be a chemically unmodified hydrolysed protein. The term ‘chemically unmodified hydrolysed protein’ means a protein that has not been further chemically modified (or reacted) other than by hydrolysis. Hydrolysed polymers may be modified by more than one functional group. Alternatively, the bulk hydrolysed protein may comprise a mixture of proteins modified by different functional groups.

Modification may comprise reacting at least 20% of the protein with a functional group, preferably more than 30%, more preferably more than 40%.

Where present, the modification agent may represent from 6 to 30 wt.% of the total copolymerisation reagents. Preferably, from 8 wt.% to 25 wt.% of the reagents. More preferably, from 10 wt.% to 20 wt.%.

The hydrolysed protein may comprise crosslinking. The crosslinking agents may preferably be di- or tri- glycidyl ethers. Said di- or tri- glycidyl ethers may be optionally alkoxylated.

Suitable di -glycidyl ethers may be selected from bisphenol A diglycidyl ether, 1,4- butanediol diglycidyl ether, 1,4-cyclohexanedimethanol diglycidyl ether, ethylene glycol diglycidyl ether, diethylene glycol diglycidyl ether, diglycidyl ether, diglycidyl resorcinol ether, 1,6-hexanediol diglycidyl ether, and neopentyl glycol diglycidyl ether. Preferably, selected from diglycidyl ether, and neopentyl glycol diglycidyl ether.

Suitable tri-glycidyl ethers may be selected from castor oil glycidyl ether, trimethylolethane trigly cidyl ether, and trimethylolpropane triglycidyl ether.

In particular, where crosslinking agents are selected based on a desire for high biobased content, crosslinkers selected from glycerol polyglycidyl ether, polyglycerol polyglycidyl ether, polyglycerol polyglycidyl ether, and sorbitol polyglycidyl ether may be selected, such as those obtainable from Nagase ChemteX of Japan. The biobased carbon content may preferably at least 70% biobased on the basis of the total weight of the carbon-containing parts of the composition, more preferably at least The level of biobased content of the compound may be determinable by the standardised analytical method ASTM D6866 using ¹⁴C radiocarbon dating. ASTM D6866 distinguishes carbon resulting from bio-based inputs from those derived from fossil-based inputs. Using this standard, a percentage of carbon from renewable sources can be calculated from the total carbon in the sample.

The di- or tri- glycidyl ethers may be alkoxylated. Alkoxylation of the di- or tri- glycidyl ethers of the present invention comprises use of oxyalkylene groups which are oxy ethylene units (-CH2CH2-O-) and/or oxypropylene units (-CH2(CH3)CH2-O-).

Each oxyalkyene group may comprise oxyethylene, oxypropylene, or a mixture of oxyethylene, oxypropylene units. Where the oxyalkylene chain comprises both oxyethylene and oxypropylene, the oxyalkylene chain may be a block or random copolymer (either normal or reverse) of oxyethylene and oxypropylene units.

The number of moles of oxyethylene and oxypropylene present in each oxyalkylene group may independently be an integer in the range from 2 to 20. For example, it will be understood where the value of is 2 there are two moles of oxyethylene and/or oxypropylene present in that specific oxyalkylene chain.

The total number of moles of oxyethylene or oxypropylene units present in each crosslinking molecule may be an integer value in the range of from 2 to 20. Preferably, in the range from 2 to 18. More preferably, in the range from 4 to 14. Further preferably, in the range from 4 to 12. Most preferably, in the range from 6 to 10. Therefore, preferably the oxyalkylene group is formed of in the range from 4 to 12 oxy ethylene units, and most preferably in the range from 6 to 10 oxy ethylene units.

Where present, the crosslinking agents may represent from 4 to 55 wt.% of the total copolymerisation reagents. Preferably, from 6 wt.% to 50 wt.% of the reagents. More preferably, from 8 wt.% to 40 wt.%. Specific preferred examples of alkoxylated di- and tri- glycidyl ethers may be selected from polyethylene glycol diglycidyl ether and polypropylene glycol diglycidyl ether.

In particular, polyethylene glycol (500) diglycidyl ether and polypropylene glycol (380) diglycidyl ether may be especially preferred. It will be understood that 500 represents the number average molecular weight (M_n).

It is envisaged that crosslinking may be combined with copolymerisation and/or chemical modification. Preferably, crosslinked dispersants may be based on hydrolysed proteins which have not been chemically modified and are not copolymers.

A further advantage of crosslinking may be that the resulting dispersant may be biodegradable. The term ‘biodegradable’ is used herein to mean proteins which have been subject to degradation and hydrolysed. The hydrolysed protein may comprise protein fragments, polypeptides, peptides, amino acids and/or peptones.

The hydrolysed protein with crosslinking may be biodegradable. Preferably, at least 50% of said dispersants within a 28 day period in accordance with the OECD methods 301B and 301F. More preferably, at least 60%. Most preferably, at least 70%.

The hydrolysed protein with crosslinking may therefore have the advantage from prior compounds used for this function in being more biodegradable, and therefore more sustainable.

The hydrolysed protein used herein, without copolymerisation or modification, may suitably has a molecular weight (weight average) in the range preferably from 5,000 to 1,000,000, preferably 5,000 to 400,000, more preferably 12,000 to 300,000, particularly 15,000 to 280,000, and especially 17,000 to 260,000. If copolymerised, the copolymer used herein suitably has a molecular weight (weight average) in the range preferably from 10,000 to 400,000, more preferably 12,000 to 300,000, particularly 15,000 to 280,000, and especially 17,000 to 260,000.

If copolymerised and modified, the modified copolymer used herein suitably has a molecular weight (weight average) in the range preferably from 1,000 to 40,000, preferably 10,000 to 120,000, more preferably 12,000 to 100,000, particularly 15,000 to 80,000, and especially 17,000 to 60,000.

If crosslinked, the crosslinked hydrolysed protein used herein suitably has a molecular weight (weight average) in the range preferably from 5,000 to 800,000, preferably 5,000 to 400,000, more preferably 12,000 to 200,000, particularly 15,000 to 100,000, particularly 17,000 to 260,000, and especially 30,000 to 130,000.

The molecular weight (weight average) of the polymeric binders described herein can is determined by HPLC (SE-HPLC) as described herein, specifically the TSKgel GMPWXL Protocol.

The hydrolysed protein may comprise other monomer units. In particular monomers originating from initiator used in making the hydrolysed protein where copolymerised may be present.

The initiator may be selected from azo polymerisation initiators or peroxide initiators. Azo polymerisation initiators may be preferred. It will be understood that azo polymerisation initiators are known as compounds having an azo group (R-N=N-R'), which decomposes with heat and/or light, and forms carbon radical, and are generally known in the field of polymerisation as having initiator function.

Preferred peroxide initiators may be selected from tert-butyl peroxide and hydroperoxide. Preferably suitable azo initiators may be water soluble, and selected from 2,2'- Azobis[2-(2-imidazolin-2-yl)propane]dihydrochloride, 2,2'-Azobis(2- methylpropionamidine)dihydrochloride, 4,4'-Azobis(4-cyanovaleric acid), 2,2'- Azobis[2-(2-imidazolin-2-yl)propane], 2,2'-Azobis[N-(2-carboxyethyl)-2- methylpropionamidine]tetrahydrate, or a combination thereof. Most preferably, the initiator may be 2,2'-Azobis(2-methylpropionamidine)dihydrochloride (V50).

Where present, the initiator may represent from 3 to 20 wt.% of the total copolymerisation reagents. Preferably, from 5 wt.% to 16 wt.% of the reagents. More preferably, from 7 wt.% to 12 wt.%.

Preferably the amino compound is obtained from a renewable source. The amino compound is not obtained from an animal protein source. This is advantageous since animal sources can be undesirable for consumers. Preferably the composition comprises no animal-derived components. Preferably the composition comprises no petrochemical-derived components.

Preferably the carbon-containing parts of the composition are at least 40% biobased according to ASTM D6866 on the basis of the total weight of the carbon-containing parts of the composition, more preferably at least 50%, particularly at least 60% biobased.

Agrochemical actives for use in the formulations according to the invention are solid agrochemical active. These are agrochemically active compounds are solid, and this may include actives which are relatively insoluble in water at room temperature and may also therefore be hydrophobic.

In the present invention, hydrophobic solid agrochemicals means those which are very slightly soluble (lower than 5% solubility at 20°C to 25°C) or practically insoluble in water. In agrochemistry, the logarithm of the ratio of the concentrations of the unionised solute in two solvents, respectively octanol and water, is used as an index of the pesticide lipophilicity, and is known as the octanol/water coefficient, logP. The agrochemically active may have a logP value in the range 0.1 to 5. More preferably, in the range from 0.3 to 2.

Agrochemical actives refer to biocides which, in the context of the present invention, are plant protection agents, more particular chemical substances capable of killing different forms of living organisms used in fields such as medicine, agriculture, forestry, and mosquito control. Also counted under the group of biocides are so- called plant growth regulators.

Biocides for use in agrochemical formulations of the present invention are typically divided into two sub- groups:

■ pesticides, including fungicides, herbicides, insecticides, algicides, moluscicides, miticides and rodenticides, and

■ antimicrobials, including germicides, antibiotics, antibacterials, antivirals, antifungals, antiprotozoal s and antiparasites.

In particular, biocides selected from insecticides, fungicides, or herbicides may be particularly preferred.

Examples of fungicides that can be employed in the present disclosure include, but are not limited to: (3-ethoxypropyl)-mercury bromide, 2-m ethoxy ethylmercury chloride, 2-phenylphenol, 8-hydroxyquinoline sulfate, 8-phenylmercurioxyquinoline, acibenzolar, acibenzolar-S-methyl, acypetacs, acypetacs-copper, acypetacs-zinc, aldimorph, allyl alcohol, ametoctradin, amisulbrom, ampropylfos, anilazine, aureofungin, azaconazole, azithiram, azoxystrobin, barium polysulfide, benalaxyl, benalaxyl-M, benodanil, benomyl, benquinox, bentaluron, benthiavalicarb, benthiavalicarb-isopropyl, benzalkomum chloride, benzamacril, benzamacril-isobutyl, benzamorf, benzohydroxamic acid, bethoxazin, binapacryl, biphenyl, bitertanol, bithionol, bixafen, blasticidin-S, Bordeaux mixture, boscalid, bromuconazole, bupirimate, Burgundy mixture, buthiobate, butylamine, calcium polysulfide, captafol, captan, carbamorph, carbendazim, carboxin, carpropamid, carvone, Cheshunt mixture, chinomethionat, chi obenthi azone, chloraniformethan, chloranil, chlorfenazole, chlorodinitronaphthalene, chloroneb, chloropicrin, chlorothalonil, chlorquinox, chlozolinate, climbazole, clotrimazole, copper acetate, copper carbonate, basic, copper hydroxide, copper naphthenate, copper oleate, copper oxychloride, copper silicate, copper sulfate, copper zinc chromate, cresol, cufraneb, cuprobam, cuprous oxide, cyazofamid, cyclafuramid, cycloheximide, cyflufenamid, cymoxanil, cypendazole, cyproconazole, cyprodinil, dazomet, dazomet-sodium, DBCP, debacarb, decafentin, dehydroacetic acid, dichlofluanid, dichlone, dichlorophen, dichlozoline, diclobutrazol, diclocymet, diclomezine, diclomezine-sodium, dicloran, diethofencarb, diethyl pyrocarbonate, difenoconazole, diflumetorim, dimethirimol, dimethomorph, dimoxystrobin, diniconazole, diniconazole-M, dinobuton, dinocap, dinocap-4, dinocap-6, dinocton, dinopenton, dinosulfon, dinoterbon, diphenylamine, dipyrithione, disulfiram, ditalimfos, dithianon, DNOC, DNOC-ammonium, DNOC- potassium, DNOC-sodium, dodemorph, dodemorph acetate, dodemorph benzoate, dodicin, dodicin-sodium, dodine, drazoxolon, edifenphos, epoxiconazole, etaconazole, etem, ethaboxam, ethirimol, ethoxyquin, ethylmercury 2,3- dihydroxypropyl mercaptide, ethylmercury acetate, ethylmercury bromide, ethylmercury chloride, ethylmercury phosphate, etridiazole, famoxadone, fenamidone, fenaminosulf, fenapanil, fenarimol, fenbuconazole, fenfuram, fenhexamid, fenitropan, fenoxanil, fenpiclonil, fenpropidin, fenpropimorph, fentin, fentin chloride, fentin hydroxide, ferbam, ferimzone, fluazinam, fiudioxonil, flumetover, flumorph, fluopicolide, fluopyram, fluoroimide, fluotrimazole, fluoxastrobin, fluquinconazole, flusilazole, flusulfamide, flutianil, flutolanil, flutriafol, fluxapyroxad, folpet, formaldehyde, fosetyl, fosetyl-aluminium, fuberidazole, furalaxyl, furametpyr, furcarbanil, furconazole, furconazole-cis, furfural, furmecyclox, furophanate, glyodin, griseofulvin, guazatine, halacrinate, hexachlorobenzene, hexachlorobutadiene, hexaconazole, hexylthiofos, hydrargaphen, hymexazol, imazalil, imazalil nitrate, imazalil sulfate, imibenconazole, iminoctadine, iminoctadine triacetate, iminoctadine trialbesilate, iodomethane, ipconazole, iprobenfos, iprodione, iprovalicarb, isoprothiolane, isopyrazam, isotianil, isovaledione, kasugamycin, kresoxim-methyl, mancopper, mancozeb, mandipropamid, maneb, mebenil, mecarbinzid, mepanipyrim, mepronil, meptyldinocap, mercuric chloride, mercuric oxide, mercurous chloride, metalaxyl, metalaxyl-M, metam, metam-ammonium, metam-potassium, metam-sodium, metazoxolon, metconazole, methasulfocarb, methfuroxam, methyl bromide, methyl isothiocyanate, methylmercury benzoate, methylmercury dicyandiamide, methylmercury pentachlorophenoxide, metiram, metominostrobin, metrafenone, metsulfovax, milneb, myclobutanil, myclozolin, N-(efhylmercury)-p-toluene- sulphonanilide, nabam, natamycin, nitrostyrene, nitrothal -isopropyl, nuarimol, OCH, octhilinone, ofurace, orysastrobin, oxadixyl, oxine-copper, oxpoconazole, oxpoconazole fumarate, oxycarboxin, pefurazoate, penconazole, pencycuron, penflufen, pentachlorophenol, penthiopyrad, phenylmercuriurea, phenylmercury acetate, phenylmercury chloride, phenylmercury derivative of pyrocatechol, phenylmercury nitrate, phenylmercury salicylate, phosdiphen, phthalide, picoxystrobin, piperalin, polycarbamate, polyoxins, polyoxorim, polyoxorim-zinc, potassium azide, potassium polysulfide, potassium thiocyanate, probenazole, prochloraz, procymidone, propamocarb, propamocarb hydrochloride, propi conazole, propineb, proquinazid, prothiocarb, prothiocarb hydrochloride, prothioconazole, pyracarbolid, pyraclostrobin, pyraclostrobin, pyrametostrobin, pyraoxystrobin, pyrazophos, pyribencarb, pyridinitril, pyrifenox, pyrimethanil, pyriofenone, pyroquilon, pyroxychlor, pyroxyfur, quinacetol, quinacetol sulfate, quinazamid, quinconazole, quinoxyfen, quintozene, rabenzazole, salicylanilide, sedaxane, silthiofam, simeconazole, sodium azide, sodium orthophenylphenoxide, sodium pentachlorophenoxide, sodium polysulfide, spiroxamine, streptomycin, sulfur, sultropen, TCMTB, tebuconazole, tebufloquin, tecloftalam, tecnazene, tecoram, tetraconazole, thiabendazole, thiadifluor, thicyofen, thifluzamide, thiochlorfenphim, thiomersal, thiophanate, thiophanate-methyl, thioquinox, thiram, tiadinil, tioxymid, tolclofos-methyl, tolylfluanid, tolylmercury acetate, triadimefon, triadimenol, triamiphos, triarimoi, triazbutil, triazoxide, tributyltin oxide, trichlamide, tricyclazole, tridemorph, trifloxystrobin, triflumizole, triforine, tri ti conazole, uniconazole, uniconazole-P, validamycin, valifenalate, vinclozolin, zarilamid, zinc naphthenate, zineb, ziram, zoxamide and mixtures thereof. Examples of insecticides that can be employed in the present disclosure include, but are not limited to: 1,2- dichloropropane, abamectin, acephate, acetamiprid, acethion, acetoprole, acrinathrin, acrylonitrile, alanycarb, aldicarb, aldoxycarb, aldrin, allethrin, allosamidin, allyxycarb, alpha-cypermethrin, alpha-ecdysone, alpha-endosulfan, amidithion, aminocarb, amiton, amiton oxalate, amitraz, anabasine, athidathion, azadirachtin, azamethiphos, azinphos-ethyl, azinphos-methyl, azothoate, barium hexafluorosilicate, barthrin, bendiocarb, benfuracarb, bensultap, beta-cyfluthrin, beta- cypermethrin, bifenthrin, bioallethrin, bioethanomethrin, biopermethrin, bistrifluoron, borax, boric acid, bromfenvinfos, bromocyclen, bromo-DDT, bromophos, bromophos-ethyl, bufencarb, buprofezin, butacarb, butathiofos, butocarboxim, butonate, butoxycarboxim, cadusafos, calcium arsenate, calcium polysulfide, camphechlor, carbanolate, carbaryl, carbofuran, carbon disulfide, carbon tetrachloride, carbophenothion, carbosulfan, cartap, cartap hydrochloride, chlorantraniliprole, chlorbicyclen, chlordane, chlordecone, chlordimeform, chlordimeform hydrochloride, chlorethoxyfos, chlorfenapyr, chlorfenvinphos, chlorfluazuron, chlormephos, chloroform, chloropicrin, chlorphoxim, chlorprazophos, chlorpyrifos, chlorpyrifos- methyl, chlorthiophos, chiOmafenozide, cinerin I, cinerin II, cinerins, cismethrin, cloethocarb, closantel, clothianidin, copper acetoarsenite, copper arsenate, copper naphthenate, copper oleate, coumaphos, coumithoate, crotamiton, crotoxyphos, crufomate, cryolite, cyanofenphos, cyanophos, cyanthoate, cyantraniliprole, cyclethrin, cycloprothrin, cyfluthrin, cyhalothrin, cypermethrin, cyphenothrin, cyromazine, cythioate, DDT, decarbofuran, deltamethrin, demephion, demephion-O, demephion-S, demeton, demeton-methyl, demeton-O, demeton-O- methyl, demeton-S, demeton-S-methyl, demeton- S-methylsulphon, diafenthiuron, dialifos, diatomaceous earth, diazinon, dicapthon, dichlofenthion, dichlorvos, dicresyl, dicrotophos, dicyclanil, dieldrin, diflubenzuron, dilor, dimefluthrin, dimefox, dimetan, dimethoate, dimethrin, dimethylvinphos, dimetilan, dinex, dinex-diclexine, dinoprop, dinosam, dinotefuran, diofenolan, dioxabenzofos, dioxacarb, dioxathion, disulfoton, dithicrofos, d-limonene, DNOC, DNOC-ammonium, DNOC-potassium, DNOC- sodium, doramectin, ecdysterone, emamectin, emamectin benzoate, EMPC, empenfhrin, endosulfan, endothion, endrin, EPN, epofenonane, eprinomectin, esdepallethrine, esfenvalerate, etaphos, ethiofencarb, ethion, ethiprole, ethoate- methyl, ethoprophos, ethyl formate, ethyl-DDD, ethylene dibromide, ethylene dichloride, ethylene oxide, etofenprox, etrimfos, EXD, famphur, fenamiphos, fenazaflor, fenchlorphos, fenethacarb, fenfluthrin, fenitrothion, fenobucarb, fenoxacrim, fenoxycarb, fenpirithrin, fenpropathrin, fensulfothion, fenthion, fenthion- ethyl, fenvalerate, fipronil, flonicamid, flubendiamide, flucofuron, flucycloxuron, flucythrinate, flufenerim, flufenoxuron, flufenprox, fluvalinate, fonofos, formetanate, formetanate hydrochloride, formothion, fomiparanate, fomiparanate hydrochloride, fosmethilan, fospirate, fosthietan, fufenozide, furathiocarb, furethrin, gamma- cyhalothrin, gamma- HCH, halfenprox, halofenozide, HCH, HEOD, heptachlor, heptenophos, heterophos, hexaflumuron, HHDN, hydramethylnon, hydrogen cyanide, hydroprene, hyquincarb, imidacloprid, imiprothrin, indoxacarb, iodomethane, IPSP, isazofos, isobenzan, isocarbophos, isodrin, isofenphos, isofenphosm ethyl, isoprocarb, isoprothiolane, isothioate, isoxathion, ivermectin, jasmolin I, jasmolin II, jodfenphos, juvenile hormone I, juvenile hormone II, juvenile hormone III, kelevan, kinoprene, lambda- cyhalothrin, lead arsenate, lepimectin, leptophos, lindane, lirimfos, lufenuron, lythidathion, malathion, malonoben, mazidox, mecarbam, mecarphon, menazon, meperfluthrin, mephosfolan, mercurous chloride, mesulfenfos, metaflumizone, methacrifos, methamidophos, methidathion, methiocarb, methocrotophos, methomyl, methoprene, methothrin, methoxychlor, methoxyfenozide, methyl bromide, methyl isothiocyanate, methylchloroform, methylene chloride, metofluthrin, metolcarb, metoxadiazone, mevinphos, mexacarbate, milbemectin, milbemycin oxime, mipafox, mirex, molosultap, monocrotophos, monomehypo, monosultap, morphothion, moxidectin, naftalofos, naled, naphthalene, nicotine, nifluridide, nitenpyram, nithiazine, nitrilacarb, novaluron, noviflumuron, omethoate, oxamyl, oxydemeton- methyl, oxydeprofos, oxy di sulfoton, para-dichlorobenzene, parathion, parathion- methyl, penfluoron, pentachlorophenol, permethrin, phenkapton, phenothrin, phenthoate, phorate, phosalone, phosfolan, phosmet, phosnichlor, phosphamidon, phosphine, phoxim, phoxim-methyl, pirimetaphos, pirimicarb, pirimiphos-ethyl, pirimiphos-methyl, potassium arsenite, potassium thiocyanate, pp'-DDT, prallethrin, precocene I, precocene II, precocene III, primidophos, profenofos, profluralin, profluthrin, promacyl, promecarb, propaphos, propetamphos, propoxur, prothidathion, prothiofos, prothoate, protrifenbute, pymetrozine, pyraclofos, pyrafluprole, pyrazophos, pyresmethrin, pyrethrin I, pyrethrin II, pyrethrins, pyridaben, pyridalyl, pyridaphenthion, pyrifluquinazon, pyrimidifen, pyrimitate, pyriprole, pyriproxyfen, quassia, quinalphos, quinalphos-methyl, quinothion, rafoxanide, resmethrin, rotenone, ryania, sabadilla, schradan, selamectin, silafluofen, silica gel, sodium arsenite, sodium fluoride, sodium hexafluorosilicate, sodium thiocyanate, sophamide, spinetoram, spinosad, spiromesifen, spirotetramat, sulcofuron, sulcofuron-sodium, sulfluramid, sulfotep, sulfoxaflor, sulfuryl fluoride, sulprofos, tau-fluvalinate, tazimcarb, TDE, tebufenozide, tebufenpyrad, tebupirimfos, teflubenzuron, tefluthrin, temephos, TEPP, terallethrin, terbufos, tetrachloroethane, tetrachlorvinphos, tetramethrin, tetramethylfluthrin, theta-cypei-methiin, thiacloprid, thiamethoxam, thicrofos, thiocarboxime, thiocyclam, thiocyclam oxalate, thiodicarb, thiofanox, thiometon, thiosultap, thiosultap-disodium, thiosultap-monosodium, thuringiensin, tolfenpyrad, tralomethrin, transfluthrin, transpermethrin, triarathene, triazamate, triazophos, trichlorfon, trichlormetaphos-3, trichloronat, trifenofos, triflumuron, trimethacarb, triprene, vamidothion, vaniliprole, XMC, xylylcarb, zeta-cypermethrin, zolaprofos and mixtures thereof.

Examples of herbicides that can be employed in the present disclosure include, but are not limited to: 4-CPA, 4-CPB, 4-CPP, 2,4-D, 3,4- DA, 2,4-DB, 3,4-DB, 2,4-DEB, 2,4-DEP, 3,4-DP, 2,3,6-TBA, 2,4,5-T, 2,4,5-TB, acetochlor, acifluorfen, aclonifen, acrolein, alachlor, allidochlor, alloxydim, allyl alcohol, alorac, ametridione, ametryn, amibuzin, amicarbazone, amidosulfuron, aminocyclopyrachlor, aminopyralid, amiprofos-methyl, amitrole, ammonium sulfamate, anilofos, anisuron, asulam, atraton, atrazine, azafenidin, azimsulfuron, aziprotryne, barban, BCPC, beflubutamid, benazolin, bencarbazone, benfluralin, benfuresate, bensulfuron, bensulide, bentazone, benzadox, benzfendizone, benzipram, benzobicyclon, benzofenap, benzofiuor, benzoylprop, benzthiazuron, bicyclopyrone, bifenox, bilanafos, bispyribac, borax, bromacil, bromobonil, bromobutide, bromofenoxim, bromoxynil, brompyrazon, butachlor, butafenacil, butamifos, butenachlor, buthidazole, buthiuron, butralin, butroxydim, buturon, butylate, cacodylic acid, cafenstrole, calcium chlorate, calcium cyanamide, cambendichlor, carbasulam, carbetamide, carboxazole chiorprocarb, carfentrazone, CDEA, CEPC, chlomethoxyfen, chloramben, chloranocryl, chlorazifop, chlorazine, chlorbromuron, chlorbufam, chloreturon, chlorfenac, chlorfenprop, chlorflurazole, chlorflurenol, chloridazon, chlorimuron, chlornitrofen, chloropon, chlorotoluron, chloroxuron, chloroxynil, chlorpropham, chlorsulfuron, chlorthal, chlorthiamid, cinidon-ethyl, cinmethylin, cinosulfuron, cisanilide, clethodim, cliodinate, clodinafop, clofop, clomazone, clomeprop, cloprop, cloproxydim, clopyralid, cloransulam, CMA, copper sulfate, CPMF, CPPC, credazine, cresol, cumyluron, cyanatryn, cyanazine, cycloate, cyclosulfamuron, cycloxydim, cycluron, cyhalofop, cyperquat, cyprazine, cyprazole, cypromid, daimuron, dalapon, dazomet, delachlor, desmedipham, desmetryn, diallate, dicamba, dichlobenil, dichloralurea, dichloiTnate, dichlorprop, dichlorprop-P, diclofop, diclosulam, diethamquat, diethatyl, difenopenten, difenoxuron, difenzoquat, diflufenican, diflufenzopyr, dimefuron, dimepiperate, dimethachlor, dimethametryn, dimethenamid, dimethenamid-P, dimexano, dimidazon, dinitramine, dinofenate, dinoprop, dinosam, dinoseb, dinoterb, diphenamid, dipropetryn, diquat, disul, dithiopyr, diuron, DMPA, DNOC, DSMA, EBEP, eglinazine, endothal, epronaz, EPTC, erbon, esprocarb, ethalfluralin, ethametsulfuron, ethidimuron, ethiolate, ethofumesate, ethoxyfen, ethoxysulfuron, etinofen, etnipromid, etobenzanid, EXD, fenasulam, fenoprop, fenoxaprop, fenoxaprop-P, fenoxasulfone, fenteracol, fenthiaprop, fentrazamide, fenuron, ferrous sulfate, flamprop, flamprop-M, fl azasulfur on, florasulam, fluazifop, fluazifop-P, fluazolate, flucarbazone, flucetosulfuron, fluchloralin, flufenacet, flufenican, flufenpyr, flumetsulam, flumezin, flumiclorac, flumioxazin, flumipropyn, fluometuron, fluorodifen, fluoroglycofen, fluoromidine, fluoronitrofen, fluothiuron, flupoxam, flupropacil, flupropanate, flupyrsulfuron, fluridone, fluorochloridone, fluoroxypyr, flurtamone, fluthiacet, fomesafen, foramsulfuron, fosamine, furyloxyfen, glufosinate, glufosinate-P, glyphosate, halosafen, halosulfuron, haloxydine, haloxyfop, haloxyfop-P, hexachloroacetone, hexaflurate, hexazinone, imazamethabenz, imazamox, imazapic, imazapyr, imazaquin, imazethapyr, imazosulfuron, indanofan, indazifiam, iodobonil, iodomethane, iodosulfuron, ioxynil, ipazine, ipfencarbazone, iprymidam, isocarbamid, isocil, isomethiozin, isonoruron, isopolinate, isopropalin, isoproturon, isouron, isoxaben, isoxachlortole, isoxaflutole, isoxapyrifop, karbutilate, ketospiradox, lactofen, lenacil, linuron, MAA, MAMA, MCPA, MCPA-thioethyl, MCPB, mecoprop, mecoprop-P, medinoterb, mefenacet, mefluidide, mesoprazine, mesosulfuron, mesotrione, metam, metamifop, metamitron, metazachlor, metazosulfuron, metflurazon, methabenzthiazuron, methalpropalin, methazole, methiobencarb, methiozolin, methiuron, methometon, methoprotryne, methyl bromide, methyl isothiocyanate, methyldymron, metobenzuron, metobromuron, metolachlor, metosulam, metoxuron, metribuzin, metsulfuron, molinate, monalide, monisouron, monochloroacetic acid, monolinuron, monuron, morfamquat, MSMA, naproanilide, napropamide, naptalam, neburon, nicosulfuron, nipyraclofen, nitralin, nitrofen, nitrofluorfen, norflurazon, noruron, OCH, orbencarb, orthodichlorobenzene, orthosulfamuron, oryzalin, oxadiargyl, oxadiazon, oxapyrazon, oxasulfuron, oxaziclomefone, oxyfluorfen, parafluoron, paraquat, pebulate, pelargonic acid, pendimethalin, penoxsulam, pentachlorophenol, pentanochlor, pentoxazone, perfluidone, pethoxamid, phenisopham, phenmedipham, phenmedipham-ethyl, phenob enzuron, phenylmercury acetate, picloram, picolinafen, pinoxaden, piperophos, potassium arsenite, potassium azide, potassium cyanate, pretilachlor, primisulfuron, procyazine, prodiamine, profluazol, profluralin, profoxydim, proglinazine, prometon, prometryn, propachlor, propanil, propaquizafop, propazine, propham, propisochlor, propoxycarbazone, propyrisulfuron, propyzamide, prosulfalin, prosulfocarb, prosulfuron, proxan, prynachlor, pydanon, pyraclonil, pyraflufen, pyrasulfotole, pyrazolynate, pyrazosulfuron, pyrazoxyfen, pyribenzoxim, pyributicarb, pyriclor, pyridafol, pyridate, pyriftalid, pyriminobac, pyrimisulfan, pyrithiobac, pyroxasulfone, pyroxsulam, quinclorac, quinmerac, quinoclamine, quinonamid, quizalofop, quizalofop-P, rhodethanil, rimsulfuron, saflufenacil, S- metolachlor, sebuthylazine, secbumeton, sethoxydim, siduron, simazine, simeton, simetryn, SMA, sodium arsenite, sodium azide, sodium chlorate, sulcotrione, sulfallate, sulfentrazone, sulfometuron, sulfosulfuron, sulfuric acid, sulglycapin, swep, TCA, tebutam, tebuthiuron, tefuryltrione, tembotrione, tepraloxydim, terbacil, terbucarb, terbuchlor, terbumeton, terbuthylazine, terbutryn, tetrafluoron, thenylchlor, thiazafluoron, thiazopyr, thidiazimin, thidiazuron, thiencarbazone-methyl, thifensulfuron, thiobencarb, tiocarbazil, tioclorim, topramezone, tralkoxydim, tri- allate, triasulfuron, triaziflam, tribenuron, tricamba, triclopyr, tridiphane, trietazine, trifloxysulfuron, trifluralin, triflusulfuron, trifop, trifopsime, trihydroxytriazine, trimeturon, tripropindan, tritac tritosulfuron, vernolate, xylachlor and mixtures thereof. [0020] Safeners mean active ingredients applied with herbicides to protect crops against their injury. Some of the safeners that can be employed in the present disclosure include, but are not limited to: benoxacor, benthiocarb, brassinolide, cloquintocet (mexyl), cyometrinil, daimuron, dichlormid, dicyclonon, dimepiperate, disulfoton, fenchlorazole-ethyl, fenclorim, flurazole, fluxofenim, furilazole, isoxadifen-ethyl, mefenpyr-di ethyl, MG 191, MON 4660, naphthalic anhydride (NA), oxabetrinil, R29148, N-phenylsulfonylbenzoic acid amides and mixtures thereof.

Most preferably, the active present in the agrochemical formulation of the present invention may be selected from imidacloprid, diflufenican, azoxystrobin, or trifloxystrobin.

Agrochemically active compounds, including insecticides and fungicides, require a formulation which allows the active compounds to be taken up by the plant/the target organisms.

The term ‘agrochemical formulation’ as used herein refers to compositions including an active agrochemical, and is intended to include all forms of compositions, including concentrates and spray formulations. If not specifically stated, the agrochemical formulation of the present invention may be in the form of a concentrate, a diluted concentrate, or a sprayable formulation.

The dispersant of the present invention may be combined with other components in order to form an agrochemical formulation comprising at least one agrochemical active.

The formulations of the present invention are water based suspension type formulations. In the concentrate form these are generally used to disperse water insoluble active ingredients where the dispersion is directly in the aqueous phase or absorbed in or adsorbed onto a solid support or as microencapsulated liquid or solutions of actives. These are commonly known as suspension concentrates (SC), in which the active compound is be present as a solid.

Additionally, the formulation of the present invention may be a suspo emulsion (SE) where two active ingredients of differing physical properties are combined in one formulation. Said suspo emulsions comprises a dispersion of insoluble solid active in to water, with dispersion of a water insoluble liquid or solution of solid in oil.

The aqueous agrochemical concentrates are agrochemical compositions designed to be diluted with water (or a water based liquid) to form the corresponding spray formulations.

Spray formulations are aqueous agrochemical formulations including all the components which it is desired to apply to the plants or their environment. Spray formulations can be made up by simple dilution of concentrates containing desired components (other than water).

The dispersants may therefore be incorporated into the formulation of the agrochemical active compound (in-can/built-in formulation).

According to the needs of the customer, concentrates thus formed may comprise typically up to 95 wt.% agrochemical actives. Said concentrates may be diluted for use resulting in a dilute composition having an agrochemical active concentration of about 0.5 wt.% to about 1 wt.%. In said dilute composition (for example, a spray formulation, where a spray application rate may be from 10 to 500 l.ha'¹) the agrochemical active concentration may be in the range from about 0.001 wt.% to about 1 wt.% of the total formulation as sprayed.

The dispersant of the present invention will typically be used in an amount proportional to the amount of the active agrochemical in the formulation. In agrochemical formulation concentrates, the proportion of the dispersant will depend on the solubility of the components in the liquid carrier. Typically, the concentration of the dispersant in such a concentrate will be from 1 wt.% to 20 wt.%. Preferably, from 1.5 wt.% to 10 wt.%. More preferably, from 2 wt.% to 5 wt.%.

The weight ratio of dispersant to active agrochemical in the concentrate and dilute concentrate agrochemical formulation is preferably from about 0.05: 1 to about 0.2: 1. More preferably, from about 0.7:1 to about 0.15: 1. This ratio range will generally be maintained for concentrate forms of formulations (e.g. where the adjuvant is included in a dispersible liquid concentrate or dispersible solid granule formulation), and in the spray formulations.

When concentrates (solid or liquid) are used as the source of active agrochemical and/or dispersant, the concentrates will typically be diluted to form the spray formulations. The dilution may be with from 1 to 10,000, particularly 10 to 1,000, times the total weight of the concentrate of water to form the spray formulation.

Where the agrochemical active is present in the aqueous end use formulation as solid particles, most usually it will be present as particles mainly of active agrochemical. However, if desired, the active agrochemical can be supported on a solid carrier e.g. silica or diatomaceous earth, which can be solid support, filler or diluent material as mentioned above.

The spray formulations will typically have a pH within the range from moderately acidic (e.g. about 3) to moderately alkaline (e.g. about 10), and particular near neutral (e.g. about 5 to 8). More concentrated formulations will have similar degrees of acidity/alkalinity, but as they may be largely non-aqueous, pH is not necessarily an appropriate measure of this.

One problem with solid actives is crystal growth e.g. by “Ostwald ripening” of the active ingredient during relatively short time of storage. Crystal growth by “Ostwald ripening” generally occurs when smaller crystals (which have a larger surface area than bigger crystals”) dissolve in the aqueous phase and the material is transported through the continuous phase, to nucleation sites of bigger crystals.

As a result, the crystals of the active ingredient may aggregate and sediment, the formulation becomes inhomogeneous; during application, filters and nozzles of the spray equipment can block and the biological efficacy may be reduced. In aqueous suspension concentrates, the aim of the dispersant is to prevent an excessive increase in crystal size.

The dispersant of the present invention has been also found to have an effect in slowing and/or stopping crystal growth in active ingredients with propensity for crystal growth through “Ostwald ripening”.

In particular the dispersant combination is of use for crystal growth inhibition for actives of particular lipophilicity - i.e. hydrophobic poorly dispersible actives. In agrochemistry, the logarithm of the ratio of the concentrations of the unionised solute in two solvents, respectively octanol and water, is used as an index of the pesticide lipophilicity, and is known as the octanol/water coefficient, Ko/w or logP. The polymer of the invention consents the preparation of an aqueous agrochemical formulation containing from 50 to 1100 g/L of at least on pesticide having logP from - 1.5 to +6.

The formulation may also comprise additional component selected from pigments, dyes, micronutrients, agrochemical actives, bulking agents, and combinations thereof.

The agrochemical formulation may include solvents (other than water) such as monopropylene glycol, oils which can be vegetable or mineral oils such as spray oils (oils included in spray formulations as non-surfactant adjuvants), associated with the first and co-adjuvants. Such solvents may be included as a solvent for the adjuvant, and/or as a humectant, e.g. especially propylene glycol. When used such solvents will typically be included in an amount of from 5 wt.% to 500 wt.%, desirably 10 wt.% to 100 wt.%, by weight of the adjuvant. Such combinations can also include salts such as ammonium chloride and/or sodium benzoate, and/or urea especially as gel inhibition aids.

The agrochemical formulation may also include other components as desired. These other components may be selected from those including:

■ binders, particularly binders which are readily water soluble to give low viscosity solutions at high binder concentrations, such as polyvinylpyrrolidone; polyvinyl alcohol; carboxymethyl cellulose; gum arabic; sugars e.g. sucrose or sorbitol; starch; ethylene-vinyl acetate copolymers, sucrose and alginates,

■ diluents, absorbents or carriers such as carbon black; talc; diatomaceous earth; kaolin; aluminium, calcium or magnesium stearate; sodium tripolyphosphate; sodium tetraborate; sodium sulphate; sodium, aluminium and mixed sodiumaluminium silicates; and sodium benzoate,

■ disintegration agents, such as surfactants, materials that swell in water, for example carboxy methylcellulose, collodion, polyvinylpyrrolidone and microcrystalline cellulose swelling agents; salts such as sodium or potassium acetate, sodium carbonate, bicarbonate or sesquicarbonate, ammonium sulphate and dipotassium hydrogen phosphate;

■ wetting agents such as alcohol ethoxylate and alcohol ethoxylate/propoxylate wetting agents;

■ dispersants such as sulphonated naphthalene formaldehyde condensates and acrylic copolymers such as the comb copolymer having capped polyethylene glycol side chains on a polyacrylic backbone;

■ emulsifiers such as alcohol ethoxylates, ABA block co polymers, or castor oil ethoxylates;

■ antifoam agents, e.g. polysiloxane antifoam agents, typically in amounts of 0.005 wt.% to 10 wt.% of the formulation;

■ viscosity modifiers such as commercially available water soluble or miscible gums, e.g. xanthan gums, and/or cellulosics, e.g. carboxy- methyl, ethyl or propylcellulose; and/or ■ preservatives and/or anti-microbials such as organic acids, or their esters or salts such as ascorbic e.g. ascorbyl palmitate, sorbic e.g. potassium sorbate, benzoic e.g. benzoic acid and methyl and propyl 4-hydroxybenzoate, propionic e.g. sodium propionate, phenol e.g. sodium 2-phenylphenate; 1,2- benzisothiazolin-3-one; or formaldehyde as such or as paraformaldehyde; or inorganic materials such as sulphurous acid and its salts, typically in amounts of 0.01 wt.% to 1 wt.% of the formulation.

The agrochemical formulation according to the present invention may also contain components, such as surfactant materials which form part of the emulsifier system. Said surfactants may include surfactant dispersants.

Adjuvants may be included in the compositions and formulations of and used in this invention. Examples include alkylpolysaccharides (more properly called alkyl oligosaccharides); fatty amine ethoxylates e.g. coconut alkyl amine 2EO; and derivatives of alk(en)yl succinic anhydride, in particular those described in PCT applications WO 94/00508 and WO 96/16930, or sorbitans as derivatives.

The formulation may comprise at least one nutrient. Nutrients refer to chemical elements and compounds which are desired or necessary to promote or improve plant growth.

Nutrients generally are described as macronutrients or micronutrients. Suitable nutrients for use in the concentrates according to the invention are micronutrient compounds, preferably those which are solid at room temperature or are partially soluble.

Micronutrients typically refer to trace metals or trace elements, and are often applied in lower doses. Suitable micronutrients include trace elements selected from zinc, boron, chlorine, copper, iron, molybdenum, and manganese. It is envisaged that the dispersant of the present invention would have broad applicability to all types of micronutrients. The micronutrients may be in a soluble form or included as insoluble solids, and may in the form of salts or chelates. Preferably, the micronutrient is in the form of a carbonate or oxide.

Preferably, the micronutrient may be selected from zinc, calcium, molybdenum or manganese, or magnesium. Particularly preferred micronutrients for use with the present invention may be selected from zinc oxide, manganese carbonate, manganese oxide, or calcium carbonate.

The amount of micronutrient in the concentrate is typically from 5 wt.% to 40 wt.%, more usually, 10 wt.% to 35 wt.%, particularly 15 wt.% to 30, % by weight based on the total concentrate.

Typically, as mixed into formulations during make up, the average particle size of solid agrochemicals is from 50 Dm to 100 Dm, but formulations are typically wet milled after mixing to reduce the average particle size to from 1 Dm to 10 Dm, more preferably from 1 Dm to 5 Dm.

The formulations of the present invention may also comprise at least one macronutrient. Macronutrients typically refer to those comprising nitrogen, phosphorus, and potassium, and include fertilisers such as ammonium sulphate, and water conditioning agents. Suitable macronutrients include fertilisers and other nitrogen, phosphorus, or sulphur containing compounds, and water conditioning agents.

Suitable fertilisers include inorganic fertilisers that provide nutrients such as nitrogen, phosphorus, potassium or sulphur. Examples of such fertilisers include: for nitrogen as the nutrient: nitrates and or ammonium salts such as ammonium nitrate, including in combination with urea e.g. as uran type materials, calcium ammonium nitrate, ammonium sulphate nitrate, ammonium phosphates, particularly mono-ammonium phosphate, di-ammonium phosphate and ammonium polyphosphate, ammonium sulphate, and the less commonly used calcium nitrate, sodium nitrate, potassium nitrate and ammonium chloride; for phosphorus as the nutrient: acidic forms of phosphorus such as phosphoric, pyrophosphoric or polyphosphoric acids, but more usually salt forms such as ammonium phosphates, particularly mono-ammonium phosphate, di-ammonium phosphate, and ammonium polyphosphate, potassium phosphates, particularly potassium dihydrogen phosphate and potassium polyphosphate; for sulphur as the nutrient: ammonium sulphate and potassium sulphate, e.g. the mixed sulphate with magnesium.

Biostimulants may enhance metabolic or physiological processes such as respiration, photosynthesis, nucleic acid uptake, ion uptake, nutrient delivery, or a combination thereof. Non-limiting examples of biostimulants include seaweed extracts (e.g., ascophyllum nodosum), humic acids (e.g., potassium humate), fulvic acids, myoinositol, glycine, and combinations thereof.

The invention further includes a method of treating plants using formulations of the first aspect.

Accordingly the invention further includes methods of use including:

■ a method of killing or inhibiting vegetation by applying to the vegetation, or the immediate environment of the vegetation e.g. the soil around the vegetation, a spray formulation including at least one dispersed phase agrochemical and the adjuvant of the first aspect; and/or

■ a method of killing or inhibiting pests of plants by applying to the plants or the immediate environment of the plants e.g. the soil around the plants, a spray formulations including at least one dispersed phase agrochemical which is one or more pesticides, for example insecticides, fungicides or acaricides, and the adjuvant of the first aspect.

As used herein, the term ‘dispersant’ or ‘dispersancy’ refers to compounds which when added to an agrochemical formulation will improve the agrochemical’s desired effect. The dispersant may affect the diluent, the mixture, the active, or the target by its improvements of the active’s performance.

Preferably, the dispersant of the present invention may find use as either the sole component or principal dispersancy functioning agent when formulated directly into pesticide concentrates.

The materials of the present invention dilute more readily in agricultural concentrates and develop lower fluid viscosities in aqueous systems, either in the concentrate or upon dilution into water prior to spraying. This behaviour provides improved ease of use in both manufacturing and upon dilution of products containing them, especially in colder waters. Reduction of foam stability is also observed which reduces the need for foam control agents. The dispersant of the present invention may be added to agrochemical formulations without undesirable thickening or destabilisation.

It will be appreciated that the dispersion comprises particles of low water solubility solids and therefore the particle size and distribution is a factor which reflects the stability of the dispersion.

It is important that there is a homogeneous distribution of the particles to ensure stability of the dispersion for a longer period. Additionally, an effective dispersant ensures that the particles do not come together and cause phase separation. Therefore, a dispersion with small particle size, homogeneous particle distribution, and limited particle size growth over time, is likely to be a more stable dispersion.

In the form of a distribution of particle sizes, the particles would have a median volume particle diameter value. It will be understood that the median volume particle diameter refers to the equivalent spherical diameter corresponding to the point on the distribution which divides the population exactly into two equal halves. It is the point which corresponds to 50% of the volume of all the particles, read on the cumulative distribution curve relating volume percentage to the diameter of the particles i.e. 50% of the distribution is above this value and 50% is below. This value is referred to as the “D(v,0.5)” value and is determined as described herein.

Additionally, “D(v,0.9)” values can also be referred to, and these values would be the equivalent spherical diameter corresponding to 90% of the volume of all the particles, read on the cumulative distribution curve relating volume percentage to the diameter of the particles, i.e. they are the points where 10% of the distribution is above this value and 90% are below the value respectively.

The particle size values, used to determine the D(v,0.5), and D(v,0.9) values, are measured by techniques and methods as described in further detail herein. It will be understood that particle size values defined below are based on dispersant at a total of 2-3.5 wt.% as shown in the Examples.

It is generally known that particle sizes of 1-10 pm are preferred in order to obtain a dispersion having the desired properties.

The particles present in the dispersants of the present invention may have an initial D(v,0.5) value at 0 days in the range from 2.5pm to 8.0pm. Preferably, in the range from 3.0pm to 7.0pm. More preferably, in the range from 3.2pm to 6.0pm. Most preferably, in the range from 3.3pm to 6.0pm.

The particles present in the dispersants of the present invention may have a D(v,0.9) value at 0 days in the range from 5.0pm to 14.0pm. Preferably, in the range from 5.5pm to 12.0pm. More preferably, in the range from 6.0pm to 11.0pm.

The particles present in the dispersants of the present invention may have a D(v,0.5) value at 7 days and 54°C in the range from 1.0pm to 20.0pm. Preferably, in the range from 2.0pm to 18.0pm. More preferably, in the range from 3.0pm to 15.0pm. Most preferably, in the range from 3.5pm to 13.0pm. The particles present in the dispersants of the present invention may have a D(v,0.9) value at 7 days and 54°C in the range from 5.0pm to 75.0pm. Preferably, in the range from 6.0pm to 65.0pm. More preferably, in the range from 7.0pm to 62.0pm. Most preferably, in the range from 9.0pm to 60.0pm.

The particles present in the dispersants of the present invention, have a change in any or both of D(v,0.5) and D(v,0.9) between 0 days and 7 days when kept at 54°C of no more than 150%, preferably no more than 130%, most preferably no more than 110%.

The dispersants of the present invention therefore provides good particle size and particle size distribution in a range desirable for an suspension concentrate. In addition, the suspensions of the present invention maintain the desired particle sizes and particle size distribution under storage over time. i.e. there is little decrease in particle size over time.

All of the features described herein may be combined with any of the above aspects, in any combination.

In order that the present invention may be more readily understood, reference will now be made, by way of example, to the following description.

It will be understood that all tests and physical properties listed have been determined at atmospheric pressure and room temperature (i.e. 25°C), unless otherwise stated herein, or unless otherwise stated in the referenced test methods and procedures.

Examples

The following test methods were used to determine performance of the dispersant compositions.

Particle size values - the D(v0.5) and D(v0.9) values were determined by dynamic light scattering analysis using a Malvern Mastersizer 3000 with Hydro 3000SM attachments running on de-ionised water set at 2,500 rpm. The refractive index of the material was set as per the reference values below with an absorbance of 0.1, 15,000 snaps were taken over 15 seconds to obtain the data. From the particle size values obtained D(v0.5) and D(v0.9) values were readily determined.

Refractive index reference values for: Imidacloprid -1.713 refractive index used, Trifloxystrobin - 1.511 refractive index used.

■ Stability - the stability of all formulations was assessed after the stated time period at room temperature (RT, 25°C) and 54°C. All samples were visually assessed to measure sedimentation/creaming that may have occurred.

■ Suspensibility - Sample was assessed as per CIPAC MT 161. The method preparing 250 ml of aqueous diluted suspension concentrate mixed with thirty inversions of the measuring cylinder, allowing it to stand for a specified time in the cylinder (30 minutes) under defined conditions, and removing the top nine-tenths. The remaining tenth was then assayed either chemically, gravimetrically or by solvent extraction. The method gives an index of the stability of the homogeneity of the diluted suspension concentrate over time. Complete stability of the homogeneity corresponds to 100%.

■ pH - measured as a concentrate formulation according to CIPAC MT 75.

■ Weight average molecular weight - was determined by Size-Exclusion High- Performance Liquid Chromatography (SE-HPLC). The HPLC apparatus and settings used are given below.

HPLC (SE-HPLC) apparatus and settings - TSKgel GMPWXL Protocol

Synthesis methods for production materials:

• Method for hydrolysed potato protein (C7)

Potato protein isolate powder was dispersed in water. To the slurry peracetic acid was added and the slurry was stirred for 24 hours. The peracetic acid was removed from the solution by repeat sediment washing with fresh water. The acid treated potato slurry was then raised to pH >12.5 using NaOH (25%). The slurry was then stirred for 24 hours before the pH was reduced to 9.0 and any undissolved material is removed. The soluble protein was then precipitated at pH 4 and sediment washed with fresh water. Once washed the precipitate was dissolved by raising the pH to 6 using NaOH (25%). The solution was then preserved to prevent microbial growth.

• Method for potato protein (Cl)

Potato protein (400 g) was mixed into water (2800 g) and heated to 40 °C. NaOH (25%, 250 g) was added and the reaction was stirred at temperature for 22 hours. Hydrogen Peroxide (35%, 34.5 g) was added and the reaction was stirred for 45 minutes before the peroxide addition was repeated. The reaction was stirred for 1 hr 15 before the heat was turned off and HC1 (28%) was added to reduce the pH to 9.5. The reaction was filtered to remove any insoluble material. The material was adjusted to pH 4.0 with HC1 (28%) to precipitate the protein. Water was added to increase to volume of the reaction to 5000 ml. The protein was left to settle overnight before the water was removed and the solids were redissolved by raising the pH to 6.0 with NaOH (25%). The final product was preserved then filtered.

The hydrolysed potato protein (250 g) was mixed with vinyl pyrrolidinone (15.0 g) and heated to 85 °C. In a separate 50 mL beaker, 4,4'-Azobis(4-cyanovaleric acid) (5.0 g) was added to 25 ml of distilled water. NaOH (25%) was slowly stirred in to raise the pH of the initiator solution to 6.0 to dissolve the powder. Once dissolved the initiator solution was fed into the reaction over 3 hours. Once the initiator feed was complete the reaction was stirred at temperature for 3 more hours. The reaction was allowed to cool, then filtered.

Method for potato protein/poly vinyl pyrrolidone (C2)

Base Hydrolysate Preparation - To a 1 litre beaker potato protein isolate (100 g) was added along with water (500 g). The slurry was mixed and heated to 40°C. To the slurry, NaOH (25%, 75 g) was added and the reaction was covered and stirred for 22 hours. Hydrogen peroxide (35%, 6 g) was then added and after 1 hour more hydrogen peroxide (35%, 6 g) was added. The reaction was stirred for 1 hour before HC1 (28%) was added to reduce the pH to 10. Insoluble material was removed by centrifugation and more HC1 (28%) was added to precipitate the protein at pH 4.0. The precipitate was washed with fresh water before being redissolved by adding NaOH (25%) to raise the pH to 6.2. The protein solution was the preserved to prevent microbial growth.

In order to copolymerise with vinyl pyrrolidinone - to a 400 ml beaker a solution of the hydrolysed protein (above) (200.2 g) and vinyl pyrrolidinone (13.65 g) were added. The solution was stirred with a magnetic stirrer and heated to 75°C. A separate solution of V-50 initiator, 2,2'-Azobis(2- methylpropionamidine)dihydrochloride (5.44 g) in water (25 g) was fed into the protein/monomer solution over 3 hours. Once the feed had finished the line was flushed with water (10 g). The reaction was covered and stirred at temperature for 3 more hours before it was allowed to cool to room temperature. Once cool the solution was filtered to remove any precipitate. All protein PVP samples were made using the same methods but with varying concentrations of monomer and initiator.

• Method for copolymer of potato protein (C3)

In order to make the base protein hydrolysate - Potato protein (200 g) was mixed into water (1400 g) and heated to 50 °C. NaOH (25%, 125 g) was added, the slurry was stirred for 6 hours at temperature before the heat was turned off and hydrogen peroxide (16.5 g) was added, after 20 minutes, HC1 (28%) was added to reduce the pH to 10 and the peroxide addition was repeated. The slurry was then filtered to remove any insoluble material.

In order to modify with OSA - A portion of the hydrolysed protein (854 g) was heated to 40°C and N-octenyl succinic anhydride (10 g) was added. The pH was maintained between 10.0 and 10.5 for 6 hours before HC1 (28%) was added to reduce the pH to 4. The solids were allowed to settle overnight. The aqueous layer was removed, and extra water was added to raise the volume of the material to 400 ml. the pH was raised to 6.5 using NaOH (25%) to redissolve the solid material. The final product was preserved and filtered.

In order to make the VP copolymer - Modified potato protein (200 g) was mixed with vinyl pyrrolidinone (14.3 g) and heated to 85 °C. A solution of 4,4'-Azobis(4- cyanovaleric acid) (5.7 g) in water (35 g) adjusted to pH 6.5 was fed into the reaction over 3 hours. The reaction was then allowed to react for a further 3 hours before being allowed to cool.

Method for copolymer of chickpea protein (C4)

Base Hydrolysate Preparation - Chickpea protein isolate (200 g) was stirred into Water (1000 g) in a 2 litre beaker. The slurry was heated to 45°C and NaOH (25%, 150 g) was added. The reaction was covered and stirred for 21 hours. HC1 (28%) was added to reduce the pH to 10 and the slurry was filtered to remove any insoluble material. HC1 (28%) was then added to precipitate the protein at pH 4.0. The precipitate was washed with fresh water before the solid was redissolved by raising the pH to 10.2 using NaOH (25%).

In order to modify with OSA - to a 600 ml beaker a solution of hydrolysed protein (above)(300 g) was added and the solution was heated to 40°C. NaOH (25%) was used to raise the pH of the solution to pH 10.2. N-octenyl succinic anhydride (15.0 g) was added over 30 minutes. The pH was maintained between 10.0 and 10.2 throughout addition and for 4 hours after. After this time HC1 (28%) was added to reduce the pH to 6.5. The product was stirred overnight to dissolve all precipitate formed during pH adjustment

In order to copolymerise with vinyl pyrrolidinone - to a 400 ml beaker a solution of the above modified hydrolysed protein (200 g) and vinyl pyrrolidinone (10.0 g) were added. The solution was stirred with a magnetic stirrer and heated to 75°C. A separate solution of V-50 initiator, 2, 2'-Azobis(2 -methylpropionamidine) dihydrochloride (4.0 g) in water (20 g) was fed into the protein/monomer solution over 3 hours. Once the feed had finished the line was flushed with water (10 g). The reaction was covered and stirred at temperature for 3 more hours before it was allowed to cool to room temperature. Once cool the solution was filtered to remove any precipitate.

• Method for copolymer of hemp protein (C5)

Base Hydrolysate Preparation - To a 1 litre beaker, hemp protein isolate (150 g) and water (600 g) were mixed. The slurry was heated to 45°C and NaOH (25%, 95 g) was added. The slurry was covered and stirred at temperature for 21 hours. HC1 (28%) was then added to reduce the pH of the reaction to 10.0. The slurry was then centrifuged to remove any insoluble material before being precipitated at pH 4.0 by the addition of HC1 (28%). The precipitate was washed with fresh water before being redissolved at pH 6 by the addition of NaOH (25%). The hydrolysed protein was then preserved to prevent microbial growth. Vinyl pyrrolidinone copolymerisation - To a 250 ml beaker a solution of the above modified hydrolysed protein (100 g) and vinyl pyrrolidinone (5.0 g) were added. The solution was stirred with a magnetic stirrer and heated to 75°C. A separate solution of V-50 initiator, 2, 2'-Azobis(2 -methylpropionamidine) dihydrochloride (2.0 g) in water (15 g) was fed into the protein/monomer solution over 3 hours. Once the feed had finished the line was flushed with water (5 g). The reaction was covered and stirred at temperature for 3 more hours before it was allowed to cool to room temperature. Once cool the solution was filtered to remove any precipitate.

• Method for quaternarised potato protein (C6)

To a 600 ml beaker, hydrolysed protein (C8)(400 g) was adjusted to pH 10.2 using NaOH (25%). The solution was heated to 40°C and 2,3- epoxypropyltrimethylammonium chloride (70%, 9.0 g) was added. The pH of the reaction was maintained for 4 hours using NaOH (25%) before HC1 (28%) was added to reduce the pH to 6.5.

• Method for wheat protein crosslinked with PEG500DGE (C8)

Wheat protein (400 g) was mixed into water (1600 g) and heated to 40 °C. NaOH (25%, 248 g) was added and the reaction was stirred for 20 hrs. Hydrogen peroxide (22.5 g) was added and the reaction was stirred for 1 hour before the peroxide addition was repeat. HC1 (28%) was added to reduce the pH of the solution to 10.5. The hydrolysate was filtered to remove insoluble before being evaporated to concentrate

To crosslink the hydrolysed wheat protein (20.6% active, 300 g) was heated to 60 °C. PEG500DGE (6 g) was added to the reaction and added after 30 minutes more PEG500DGE (3 g) was added and the reaction was maintained between 10.0-10.4 for 6 hours. HC1 (28%) was added to drop the pH to 6.0 and preserved.

• Method for potato protein crosslinked with PEG500DGE (C9)

Potato protein (100 g) was stirred into water (700 g) and heated to 60 °C. NaOH (25%, 65 g) was added. The high pH reaction was stirred for 6 hours before HC1 (28%) was added to reduce the pH to 11.0. The heat was turned off and hydrogen peroxide (8.6 g) was added. After 30 minutes the peroxide addition was repeated. This material was filtered to remove any insolubles. The cloudy solution was then heated to 60 °C and PEG500DGE (10 g) was added, the pH was kept between 10.0- 10.4 using NaOH (25%). After 1 hr the PEGDGE addition was repeated and the reaction was stirred at temperature for 24 hrs. After 24hrs the pH was dropped to 5.5 and the final material was evaporated to RI 30 and preserved.

• Method for wheat protein crosslinked with NPDGE (CIO)

Potato protein (400 g) was mixed into water (2800 g) and heated to 40 °C. NaOH (25%, 250 g) was added and stirred at temperature for 22 hours. Hydrogen Peroxide (35%, 34.5 g) was added and the reaction was stirred for 45 minutes before the peroxide addition was repeated. The reaction was stirred for 1 hr 15 before the heat was turned off and HC1 (28%) was added to reduce the pH to 9.5. The reaction was filtered to remove any insoluble material. A portion of this material (600 g) was heated to 60 °C and adjusted to pH 10.5. NPDGE (6.5 g) was added and after 1 hour a further amount of NPDGE (6.5 g) was added. The reaction was then stirred for 18 hours at 40 °C. The pH of the reaction was then dropped to 4.0 using HC1 (28%) to precipitate the crosslinked protein. The aqueous layer was removed and the solid was redissolved by raising the pH to >6. The final product was preserved.

• Method for potato protein crosslinked with NPDGE (Cl 1)

Base protein hydrolysate - Potato protein (400 g) was mixed into water (2800 g) and heated to 40 °C. NaOH (25%, 250 g) was added and stirred at temperature for 22 hours. Hydrogen Peroxide (35%, 34.5 g) was added and the reaction was stirred for 45 minutes before the peroxide addition was repeated. The reaction was stirred for 1 hr 15 before the heat was turned off and HC1 (28%) was added to reduce the pH to 9.5. The reaction was filtered to remove any insoluble material. The material was adjusted to pH 4.0 with HC1 (28%) to precipitate the protein. Water was added to increase to volume of the reaction to 5000 ml. The protein was left to settle overnight before the water was removed and the solids were redissolved by raising the pH to 6.0 with NaOH (25%). The reaction was then preserved Crosslinking - Hydrolysed potato protein (150 g) was heated to 60 °C and adjusted to pH 10.2. NPDGE (1.5 g) was added and the reaction was stirred at temperature and controlled pH for 24 hours. The product was then precipitated at pH 4 using HC1 (28%). The aqueous layer was removed and the solid was redissolved at pH 6 and preserved.

• Method for wheat protein crosslinked with NPDGE (Cl 2)

Wheat protein (100 g) was mixed into water (700 g) and heated to 40 °C. NaOH (25%) (65 g) was added and the reaction was stirred for 18 hours. Any insoluble were removed via filtration the pH was adjusted to pH 10.2, heated to 60 °C and NPDGE (20 g) was added. The reaction was stirred for 18 hours before being precipitated at pH 2.0. The solid was recovered, redissolved at pH 6.0 and preserved.

Method for potato protein crosslinked with BDGE (Cl 3)

Potato protein (200 g) was mixed into water (1400 g) and heated to 50 °C. NaOH (25%, 125 g) was added, the slurry was stirred for 6 hours at temperature before the heat was turned off and hydrogen peroxide (35%, 16.5 g) was added. After 20 minutes, HC1 (28%) was added to reduce the pH to 10 and the peroxide addition was repeated. The slurry was then filtered to remove any insoluble material. Part of the hydrolysed protein (860g) was heated to 60 °C and BDGE (10 g) was added. After 1 hour, the BDGE (10 g) addition was repeated and the reaction was stirred for 6 hours. The pH was maintained between 10.0 and 10.5 throughout. The pH of the solution was dropped to 4.0 to precipitate the protein. The aqueous layer was removed and the solids layer was redissolved by increasing the pH to 6.4 using NaOH (25%) and preserved.

Materials produced

By the above detailed methods, the following hydrolysed proteins were produced for testing: • Cl - copolymer of potato protein/poly vinyl pyrrolidone, molecular weight around 196,000 daltons, activity around 16%

• C2 - copolymer of potato protein/poly vinyl pyrrolidone, molecular weight around 18,000 daltons, activity around 17.5%

• C3 - copolymer of potato protein/octyl succinic anhydride poly vinyl pyrrolidone, molecular weight around 43,000 daltons, activity around 21%

• C4 - copolymer of chickpea protein/octyl succinic anhydride poly vinyl pyrrolidone, molecular weight around 38,000 daltons, activity around 24%

• C5 - copolymer of hemp protein/poly vinyl pyrrolidone, molecular weight around 159,000 daltons, activity around 22%

• C6 - quaternarised potato protein, molecular weight around 10,200 daltons, activity around 14%

• C7 - hydrolysed potato protein, molecular weight around 71,000 daltons, activity around 11%

• C8 - wheat protein crosslinked with PEG500DGE, molecular weight around 50,850 daltons, activity around 21.3%

• C9 - potato protein crosslinked with PEG500DGE, molecular weight around 21,095 daltons, activity around 20.8%

• CIO - potato protein crosslinked with NPDGE, molecular weight around 90,128 daltons, activity around 14.19%

• Cl l - potato protein crosslinked with NPDGE, molecular weight around 52,294 daltons, activity around 20.45%

• C12 - wheat protein crosslinked with NPDGE, molecular weight around 34,832 daltons, activity around 16%

• C13 - potato protein crosslinked with BDGE, molecular weight arounds 77,000 daltons, activity around 19 %

NPDGE - neopentyl glycol diglycidyl ether.

PEG500DGE - polyethylene glycol (500) diglycidyl ether.

BDGE - butylene glycol diglycidyl ether

VP - N-vinyl pyrrolidinone Testing with Imidacloprid

The copolymers formed above were used to formulate a 550 g/L Imidacloprid suspension concentrate (SC) as per Table 1 below, with low levels of dispersant and wetter. Xanthan gum (typically used for structuring) was omitted.

Table 1 - 550 g/L Imidacloprid recipe

Testing with trifloxystrobin The copolymers formed above were used to formulate a 500 g/L Trifloxystrobin SC as per Table 2 below, with low levels of dispersant and wetter. Xanthan gum (typically used for structuring) was omitted.

Table 2 - 500 g/L Trifloxystrobin recipe

Testing with diflufenican

The dispersant formed above were used to formulate a 500 g/L Diflufenican SC as per

Table 3 below, with low levels of dispersant and wetter. Xanthan gum (typically used for structuring) was omitted.

Table 3 - 500 g/L Diflufenican recipe

Results The formulations (Imidacloprid, Trifl oxystrobin, and Diflufenican) were then tested over 7 days at room temperature (RT) and 54 °C as outlined in the testing schedule in Table 3 below:

Table 4 - Testing schedule

The results obtained were as follows in Table 5 to 8.

Table 5 - Results of Imidacloprid formulation for Cl, C2, C4, C7, C8

Table 6 - Results of Imidacloprid formulation C9 to C13

Table 7 - Results of Trifloxystrobin formulation C3, C5, & C6

Table 8 - Results of Diflufenican formulations Cl, C9, & C12

Biodegradation

Samples were tested for biodegradation, with results given in relation to the OECD standards as noted in Table 9.

Table 9 - Biodegradability catergorisation

The results obtained are shown in Table 10.

Table 10 - Results of biodegradability for Cl, C4, CIO, & C12

All samples tested showed high levels of biodegradability.

The proteins show excellent performance as with regard to suspensibiity and storage stability. Particle size performance shows good control over 7 days, prevention of flocculation, with limited growth, and D (0.9) of less than 10 microns. Additionally, rheology performance was observed as good.

It is to be understood that the invention is not to be limited to the details of the above embodiments, which are described by way of example only. Many variations are possible.

Claims

Claims

1. A suspension type water medium agrochemical formulation comprising; i) a hydrolysed vegetable protein dispersant, said protein having molecular weight of at least 5,000 Da; and ii) at least one solid agrochemical active dispersed in aid water medium.

2. The formulation according to claim 1, wherein the hydrolysed protein is derived from potato protein, hemp protein, and chickpea protein.

3. The formulation according to claim 2, wherein the weight average molecular weight (Mw) of the hydrolysed potato, wheat, or chickpea protein is in the range from 8,000 Da to 130,000 Da.

4. The formulation according to any preceding claim, wherein the hydrolysed protein is derived from potato protein.

5. The formulation according to any preceding claim, wherein the hydrolysed protein is copolymerised with a hydrophilic polymer selected from polyvinylpyrrolidone (PVP), polyvinyl alcohols, polyvinyl alcohol copolymers, polyglycol alkylacrylates, polyethers, polyether alkyl methacrylates, polyvinyl acetates, and polyvinyl acetate copolymers.

6. The formulation according to claim 5, wherein the hydrophilic polymer is selected from polyvinylpyrrolidone, poly vinyl alcohols, poly glycol methacrylate (HEMA), and poly (ethylene glycol) methyl ether methacrylate (PEGMA).

7. The formulation according to any preceding claim, wherein the hydrolysed protein is chemically modified by covalently reacting with a functional group selected from silicones, or alkenyl succinic anhydride.

8. The formulation according to any preceding claim, wherein the hydrolysed protein comprises crosslinking, and the crosslinking agents are di- or tri- glycidyl ethers which are optionally alkoxylated.

9. The formulation according to claim 8, wherein the crosslinking agents are selected from bisphenol A diglycidyl ether, 1,4-butanediol diglycidyl ether, 1,4- cyclohexanedimethanol diglycidyl ether, ethylene glycol diglycidyl ether, diethylene glycol diglycidyl ether, diglycidyl ether, diglycidyl resorcinol ether, 1,6-hexanediol diglycidyl ether, neopentyl glycol diglycidyl ether, castor oil glycidyl ether, trimethylolethane triglycidyl ether, and trimethylolpropane triglycidyl ether.

10. The formulation according to either claim 8 or claim 9, wherein the crosslinking agents are selected from glycerol polyglycidyl ether, polyglycerol polyglycidyl ether, polyglycerol polyglycidyl ether, and sorbitol polyglycidyl ether.

11. The formulation according to any of claims 8 to 10, wherein the crosslinked hydrolysed protein has a molecular weight (weight average) in the range from 12,000 to 200,000.

12. A concentrate formulation suitable for making an agrochemical formulation in accordance with any of claims 1 to claim 10, said concentrate comprising; i) a hydrolysed vegetable protein dispersant, said protein having molecular weight of at least 5,000 Da; and ii) at least one solid agrochemical active dispersed in aid water medium.

13. A concentrate formulation according to claim 12, wherein the formulation is an suspension concentrate (SC), or suspoemulsion (SE).

14. Use of a hydrolysed protein in accordance with claim 1, as a dispersant in an agrochemical formulation comprising solid agrochemical active.

15. A method of treating vegetation to control pests, the method comprising applying a formulation according to any of claims 1 to 11, and/or a diluted concentrate formulation in accordance with any of claims 12 to 13, either to said vegetation or to the immediate environment of said vegetation.