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WO1995025437A1 - Procede de production d'hydrolysats vegetaux de proteines, de couleur claire - Google Patents

Procede de production d'hydrolysats vegetaux de proteines, de couleur claire Download PDF

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Publication number
WO1995025437A1
WO1995025437A1 PCT/EP1995/000944 EP9500944W WO9525437A1 WO 1995025437 A1 WO1995025437 A1 WO 1995025437A1 EP 9500944 W EP9500944 W EP 9500944W WO 9525437 A1 WO9525437 A1 WO 9525437A1
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WO
WIPO (PCT)
Prior art keywords
protein
extraction
vegetable
adsorbents
flour
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP1995/000944
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German (de)
English (en)
Inventor
Edith Von Kries
Eberhard Eilers
Andreas Sander
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Publication of WO1995025437A1 publication Critical patent/WO1995025437A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/32—Protein hydrolysates; Fatty acid condensates thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/382—Vegetable products, e.g. soya meal, wood flour, sawdust

Definitions

  • the invention relates to a process for the production of vegetable protein hydrolyzates of improved color quality, in which protein-containing vegetable meal is extracted under defined conditions and the resulting protein isolates are then hydrolyzed in a manner known per se in the presence of suitable adsorbents.
  • Degradation products of polypeptides have been known for a long time. Although they have no detergent properties because of the lack of a lipophilic group, they are used in a large number of surface-active agents because of their dispersing properties and their ability to favorably influence the dermatological compatibility of anionic surfactants by interaction with the protein molecules of the skin used. Review articles on this can be found, for example, by A. Domsch et al. in doctor Cosmetol. 13, 524 (1983), G. Schuster et al. in Cosme .Toil., 99, 12 (1984) and H. Lindner in Perfume.Cosmet. , .66., 85 (1985).
  • Protein hydrolyzates based on animal collagen are usually obtained. In recent years, however, there has been a trend towards vegetable products, for example based on soybeans.
  • EP-A 0298419 discloses the production of protein hydrolyzates with an average molecular weight of 500 to 90,000 by stepwise alkaline, acidic and / or enzymatic degradation of wheat or soy proteins.
  • EP-A 0363771 reports on a process for the production of protein hydrolyzates, in which vegetable proteins are hydrolyzed with hydrochloric acid, non-hydrolyzed constituents are separated off, made alkaline to destroy undesired chlorinated compounds and the resulting products are then acidified.
  • What is common to the prior art methods, however, is that the resulting protein hydrolyzates do not meet the requirements of the market for very little colored products with regard to their color quality.
  • the object of the invention was therefore to provide such light-colored protein hydrolysates on a plant basis.
  • the invention relates to a method for producing light-colored vegetable protein hydrolyzates, in which
  • the method according to the invention includes the knowledge that vegetable proteins have a minimum solubility in the vicinity of their isoelectric point or area. Accordingly, the extraction of the protein from the protein-containing vegetable meal can be carried out at a pH either below or above the isoelectric range of the protein. In practice, for example, an alkaline extraction at pH values in the range from 8 to 14 and preferably 8.5 to 10 comes into consideration. With regard to the color quality of the resulting hydrolysates, however, acid extraction at pH values in the range from 1 to 3 and preferably 2 to 2.5 has proven to be particularly advantageous.
  • the vegetable flour is first optionally in a sufficient amount of water dispersed with heating and then adjusted to the desired pH with an acid or base, preferably hydrochloric acid, citric acid or sodium hydroxide solution.
  • an acid or base preferably hydrochloric acid, citric acid or sodium hydroxide solution.
  • the protein goes into solution, while carbohydrates, fats and, above all, the undesired potential color carriers remain in the insoluble residue, which can be separated from the valuable filtrate, for example, by filter suction, filter presses or separators.
  • the extraction is carried out several times, i.e. the protein is precipitated from the filtrate obtained in the first extraction, washed, redispersed in water, redissolved with acid or base and the residue is separated off again.
  • This process can in principle be repeated in any number, but in practice it has been shown that more than three runs do not lead to any measurable color improvement in the end products.
  • the remaining insoluble residues can be extracted again, if necessary after combining.
  • a further advantageous embodiment of the method according to the invention consists in a change in pH during the extraction. This means that the extraction is carried out in two stages, ie first in the alkaline range and then in the acidic environment or vice versa.
  • the protein hydrolyzates can be further purified by ultrafiltration and / or diafiltration before the hydrolysis; such a step can also follow the hydrolysis.
  • the solids content of the aqueous solutions obtainable after extraction is determined by the amount of water required for the dispersion and is generally 5 to 40, preferably 10 to 20,% by weight. Based on the solid, the proportion of plant proteins is above 80, preferably 90 to 98% by weight.
  • the protein isolates pre-cleaned by extraction together with suitable adsorbents in the hydrolysis can also be added at the extraction stage.
  • suitable adsorbents are silica gels, aluminum oxides and preferably activated carbons, which can be used in amounts of 0.1 to 15, preferably 1 to 5% by weight, based on the nitrogen content of the protein isolates.
  • the hydrolysis of the protein iso-prepurified by extraction can be carried out in a manner known per se in an alkaline, acidic and / or enzymatic way, the latter being preferred.
  • an alkaline aqueous suspension of the protein isolate is usually mixed with suitable enzymes, for example proteases, and the adsorbent and over degraded for a period of 1 to 24 hours at the optimum temperature of the enzymes used, for example at 50 to 70 ° C. If the digestion is carried out in the presence of calcium oxide or hydroxide as the base, calcium peptides are formed which have to be filtered off from the residue.
  • the alkali peptides are desired, it is advisable to treat the calcium peptides with soda or potash solution and then to separate off the sparingly soluble calcium carbonate. It is also possible to precipitate the calcium in the form of calcium sulfate or calcium oxalate.
  • the sparingly soluble salts are preferably separated off in the presence of filter aids by means of suction filters or filter presses.
  • Aqueous protein hydrolyzate solutions are obtained which, if necessary, can be concentrated, for example using downdraft evaporators.
  • the hydrolysates obtainable by the process according to the invention have an average molecular weight in the range from 100 to 30,000, preferably 100 to 10,000 and in particular 2000 to 5000 and a solids content of about 5 to 50% by weight.
  • the vegetable protein hydrolyzates obtainable by the process according to the invention are distinguished by a particularly advantageous color quality.
  • Another object of the invention relates to their use as ingredients of surface-active agents, for example as soil dispersants in liquid detergents or components which improve skin tolerance in cosmetic products.
  • the invention relates to their use for the production of light-colored vegetable secondary products such as, for example, N-acylated, N-alkylated, esterified and N-acylated or N-alkylated and also esterified protein hydrolyzates.
  • soy flour protein content: approx. 48% by weight
  • the aqueous protein solution from Example 1 was adjusted to a pH of 4.5 by adding sodium hydroxide solution and the soy protein was precipitated.
  • the backlog was
  • Example 4 Analogously to Example 1, 400 kg of almond flour (protein content approx. 42% by weight) were suspended in 4000 l of water, adjusted to a pH of 2 using hydrochloric acid and then separated using a separator.
  • Example 4 t
  • Example 2 Analogously to Example 1, 400 kg of wheat protein (protein content approx. 40% by weight) and 20 kg of activated carbon were suspended in 4000 l of water, adjusted to a pH of 2 using hydrochloric acid, stirred at 40 ° C. for 0.5 h and separated by a separator.
  • Example 2 Analogously to Example 1, 400 kg of potato protein (protein content approx. 45% by weight) were suspended in 4000 l of water, adjusted to a pH of 2 using hydrochloric acid and then filtered.
  • Example 7t Analogously to Example 1, 400 kg of soybean meal with the addition of 20 kg of activated carbon were suspended in 4000 l of water, adjusted to a pH of 9 with sodium hydroxide solution and stirred at 45 ° C. for 1 hour, the soy protein dissolving. The aqueous solution was then separated off from the residue using a separator. The residue was extracted again and the combined extracts processed together.
  • Example 7t
  • the aqueous protein solution from Example 6 was adjusted to a pH of 4.5 by adding hydrochloric acid and the soy protein was precipitated. The residue was washed several times, redispersed in water and dissolved again by adding sodium hydroxide solution (pH 10).
  • the pH of the mixture was adjusted to 4.2 by adding hydrochloric acid.
  • the reaction mixture was then heated to 80 ° C., a further 10 kg of activated carbon and 120 kg of filter aid (Perlite ( R) P50) were added and the mixture was stirred for 30 minutes.
  • filter aid Perlite ( R) P50
  • the reaction product was then filtered through a filter press and the filtrate was adjusted to a pH of 11.5 with calcium oxide. After a residence time of 30 min at 90 ° C., the solution was filtered, sodium carbonate solution was added and the calcium salts which had precipitated were again separated off using a filter press. The filtrate was concentrated in a downflow evaporator to a content of 41% Brix and finally filtered blank after a storage period of 3 days.
  • the Lovibond color numbers of the protein hydrolyzates were determined in a 1 cm cuvette in accordance with DIN ISO 4630 after the hydrolyzate had been stored at 40 ° C. for 4 weeks.
  • the color numbers of hydrolysates which are based on the iso- latex according to Examples 1 to 7, but without the use of active carbon in the extraction and / or hydrolysis. The results are summarized in Table 1:

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Health & Medical Sciences (AREA)
  • Zoology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Peptides Or Proteins (AREA)
  • Cosmetics (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

On obtient des hydrolysats végétaux de protéines aux couleurs de meilleure qualité, par: a) extraction de farine végétale à un pH situé en dehors de la plage isoélectrique de la protéine, éventuellement en présence d'adsorbants et par b) hydrolyse de manière alcaline, acide et/ou enzymatique, de l'hydrolysat de protéine ainsi obtenu, en présence d'adsorbants, de manière connue en soi. Ces substances s'utilisent comme constituants d'agents tensioactifs, ainsi que dans la production de dérivés tels que par exemple des produits de condensation comportant des acides gras et éventuellement modifiés de manière cationique.
PCT/EP1995/000944 1994-03-23 1995-03-14 Procede de production d'hydrolysats vegetaux de proteines, de couleur claire Ceased WO1995025437A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DEP4410000.0 1994-03-23
DE19944410000 DE4410000C1 (de) 1994-03-23 1994-03-23 Verfahren zur Herstellung hellfarbiger pflanzlicher Proteinhydrolysate

Publications (1)

Publication Number Publication Date
WO1995025437A1 true WO1995025437A1 (fr) 1995-09-28

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PCT/EP1995/000944 Ceased WO1995025437A1 (fr) 1994-03-23 1995-03-14 Procede de production d'hydrolysats vegetaux de proteines, de couleur claire

Country Status (2)

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DE (1) DE4410000C1 (fr)
WO (1) WO1995025437A1 (fr)

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1996008548A1 (fr) * 1994-09-16 1996-03-21 Henkel Kommanditgesellschaft Auf Aktien Melanges detergents doux
WO2000015655A1 (fr) * 1998-09-15 2000-03-23 Nizo Food Research Procede de production de peptides a partir de fluides biologiques et peptides produits selon ledit procede
WO2011144856A1 (fr) 2010-05-20 2011-11-24 Roquette Freres Procede de preparation d'hydrolysats alcalins de proteines vegetales
WO2012156645A1 (fr) 2011-05-16 2012-11-22 Roquette Freres Procede industriel de preparation d'hydrolysats alcalins de proteines vegetales

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE4433071C1 (de) * 1994-09-16 1995-12-21 Henkel Kgaa Milde Detergensgemische
DE19502167C2 (de) * 1995-01-25 1997-02-06 Henkel Kgaa Verfahren zur Herstellung von Reisproteinhydrolysaten
DE19502168C1 (de) * 1995-01-25 1996-06-27 Henkel Kgaa Verfahren zur Herstellung von Weizenproteinhydrolysaten
DE102009041753A1 (de) * 2009-09-16 2011-03-24 Bionorica Se Wasch-, Reinigungs- oder Desinfektionsmittel enthaltend Hydrolysate aus Pflanzenextrakten

Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
SU441915A1 (ru) * 1972-01-04 1974-09-05 Украинский Научно-Исследовательский Институт Мясной И Молочной Промышленности Способ получени белкового обогатител пищевых продуктов
EP0265099A2 (fr) * 1986-10-13 1988-04-27 Ajinomoto Co., Inc. Composition nutritive
EP0424996A2 (fr) * 1989-10-24 1991-05-02 PANZANI PONTE LIEBIG S.p.A. Hydrolyse acide des protéines végétales pour l'obtention d'un extrait protéique À  faible teneur en 3-monochloropropandiol et 1,2-dichloropropanol en quantité non-détectable
EP0466524A1 (fr) * 1990-07-13 1992-01-15 Protein Technologies International, Inc. Protéine modifiée enzymatiquement et son procédé de préparation
EP0495390A1 (fr) * 1991-01-14 1992-07-22 Cpc International Inc. Procédé de préparation des hydrolysate de protéines
JPH04335868A (ja) * 1991-05-13 1992-11-24 Kikkoman Corp 白醤油様調味料の製造法
EP0575121A1 (fr) * 1992-06-16 1993-12-22 Rohm And Haas Company Traitement de produits et de sous-produits alimentaires

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5102987A (en) * 1988-10-14 1992-04-07 Nestec S.A. Preparation of hydrolyzed protein having reduced α-chlorohydrin content

Patent Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
SU441915A1 (ru) * 1972-01-04 1974-09-05 Украинский Научно-Исследовательский Институт Мясной И Молочной Промышленности Способ получени белкового обогатител пищевых продуктов
EP0265099A2 (fr) * 1986-10-13 1988-04-27 Ajinomoto Co., Inc. Composition nutritive
EP0424996A2 (fr) * 1989-10-24 1991-05-02 PANZANI PONTE LIEBIG S.p.A. Hydrolyse acide des protéines végétales pour l'obtention d'un extrait protéique À  faible teneur en 3-monochloropropandiol et 1,2-dichloropropanol en quantité non-détectable
EP0466524A1 (fr) * 1990-07-13 1992-01-15 Protein Technologies International, Inc. Protéine modifiée enzymatiquement et son procédé de préparation
EP0495390A1 (fr) * 1991-01-14 1992-07-22 Cpc International Inc. Procédé de préparation des hydrolysate de protéines
JPH04335868A (ja) * 1991-05-13 1992-11-24 Kikkoman Corp 白醤油様調味料の製造法
EP0575121A1 (fr) * 1992-06-16 1993-12-22 Rohm And Haas Company Traitement de produits et de sous-produits alimentaires

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
DATABASE WPI Week 0193, Derwent World Patents Index; AN 93-006221 *
DATABASE WPI Week 1473, Derwent World Patents Index; AN 73-19518 *
DATABASE WPI Week 4375, Derwent World Patents Index; AN 75-71898 *
PATENT ABSTRACTS OF JAPAN vol. 017, no. 180 (C - 1046) 8 April 1993 (1993-04-08) *

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1996008548A1 (fr) * 1994-09-16 1996-03-21 Henkel Kommanditgesellschaft Auf Aktien Melanges detergents doux
WO2000015655A1 (fr) * 1998-09-15 2000-03-23 Nizo Food Research Procede de production de peptides a partir de fluides biologiques et peptides produits selon ledit procede
WO2011144856A1 (fr) 2010-05-20 2011-11-24 Roquette Freres Procede de preparation d'hydrolysats alcalins de proteines vegetales
US9149063B2 (en) 2010-05-20 2015-10-06 Roquette Freres Method for preparing alkaline hydrolysates of plant proteins
WO2012156645A1 (fr) 2011-05-16 2012-11-22 Roquette Freres Procede industriel de preparation d'hydrolysats alcalins de proteines vegetales

Also Published As

Publication number Publication date
DE4410000C1 (de) 1995-03-02

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