[go: up one dir, main page]

WO2011112100A1 - Matériau peptidique, composition alimentaire, ses préparations et ses utilisations - Google Patents

Matériau peptidique, composition alimentaire, ses préparations et ses utilisations Download PDF

Info

Publication number
WO2011112100A1
WO2011112100A1 PCT/NO2011/000079 NO2011000079W WO2011112100A1 WO 2011112100 A1 WO2011112100 A1 WO 2011112100A1 NO 2011000079 W NO2011000079 W NO 2011000079W WO 2011112100 A1 WO2011112100 A1 WO 2011112100A1
Authority
WO
WIPO (PCT)
Prior art keywords
accordance
preparation
peptide
preferable
peptide preparation
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/NO2011/000079
Other languages
English (en)
Other versions
WO2011112100A8 (fr
Inventor
Anders Aksnes
Rolf Kristian Berge
Kjartan Sandnes
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.)
Marine Bioproducts AS
Original Assignee
Marine Bioproducts AS
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 Marine Bioproducts AS filed Critical Marine Bioproducts AS
Publication of WO2011112100A1 publication Critical patent/WO2011112100A1/fr
Publication of WO2011112100A8 publication Critical patent/WO2011112100A8/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21026—Prolyl oligopeptidase (3.4.21.26), i.e. proline-specific endopeptidase
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/04—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from fish or other sea animals
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • A61K38/012—Hydrolysed proteins; Derivatives thereof from animals

Definitions

  • the present invention relates to a peptide preparation, feed compositions, a process for preparation of a peptide preparation, and uses thereof.
  • fish protein hydrolysate FPH
  • the enzymatic hydrolysing process is highly controllable, and the products are reproducible and well defined.
  • Such a protein material i.e. the fish protein hydrolysate (FPH) has several beneficial biological effects, and that such a material can be used as a pharmaceutical or nutritional material.
  • Applicant own patent application PCT/NO04/00202 discloses that the use of this FPH material lowers the concentration of plasma cholesterol and homocysteine, and also lowers the concentration of hepatic triacylglycerols.
  • PCT/N 004/00202 describes an enzyme treated fish protein hydrolysate which lowers the concentration of cholesterol in plasma, and triglycerides in the liver. FPH also induces a favourable change in the fatty acid pattern, and lowers the
  • this hydrolysate can be used as an anti-atherogenic and cardio protective agent. It is also shown that this enzyme treated fish protein hydrolysate increases the mitochondrial ⁇ -oxidation.
  • the hydrolysate is produced from fish flesh remnants on salmon bone frames after filleting, and the enzymatic hydrolysis was performed with ProtamexTM at a pH of about 6,5 and at a temperature of 55 ⁇ 2 °C, and with 60 minutes of enzymatic treatment. The resulting material is identical to the material used as control in the experiments of the present invention.
  • the present invention shows improved nutritional and medical effects compared to this (control/reference) material disclosed in PCT/NO04/00202.
  • PCT/N 004/00043 discloses a similar enzyme treated fish protein hydrolysate.
  • Protamex was used for the enzymatic treatment, and the hydrolysis was run for two hours.
  • WO06/005757 discloses a process for preparation of material where the ration of the small tripeptides IPP (lle-Pro-Pro) and VPP (Val-Pro-Pro) is at least 5.
  • Two enzymes are used, i.e. an enzyme with a proline specific endoprotease activity or prolyl oligopeptidase activity, and an enzyme which is capable of hydrolyzing the bond at the amino terminal side of a IPP-sequence.
  • US 4,940,662 discloses a method of producing a low-molecular weight peptide mixture where a first and second protease in combination with the addition of at least one amino acid pre-formed by esterification of the amino acid with an alcohol. The amino acids are incorporated into proteins by a reverse reaction of proteolysis.
  • WO06/084351 discloses anti-hypertensive tripeptides with ACE inhibitory activities were identified.
  • JP2113859 describes the use of Protease M to prepare a low-molecular peptide material.
  • WO09/128713 describes an egg-protein hydrolysate with significant DPP-IV inhibitory activity and this hydrolysate can be used for the treatment of diabetes.
  • WO94/25580 discloses a method for hydrolyzing a vegetable or animal protein by a proteolytic enzyme derived from Aspergillus oryzae where five proteolytic
  • the fish protein hydrolysate (FPH) provided by the method described in Applicant's own patent application PCT/N 004/00202 is the starting point for the improved processes, products, feed compositions and uses of the present invention, and this fish protein hydrolysate (FPH) has been treated with a second enzyme in order to improve the processes, products, feed compositions and uses thereof.
  • the specific peptide material of the present invention represents an improvement above the known fish protein hydrolysate (FPH) material that has been treated with only a primary enzymatic treatment.
  • FPH fish protein hydrolysate
  • the FPH material (control) we have used for the experimental testing is from salmon, but since the amino acid composition is fairly similar for all fish species we assume that also other non-salmon enzyme treated protein materials can be used as a basis for a second enzymatic treatment. Without being bound by theory, we believe that the mechanism of action is related to the size distribution of the peptide mixture, and not to the origin of the protein sample.
  • the peptide material in accordance with the present invention is especially useful as a functional protein in food products, particularly when used as a substitute for natural plasma in animal feeds and in pet foods.
  • additional ingredients may be added to the product such as fats, sugars, salt, flavourings, minerals, etc.
  • the product may then be formed into chunks resembling natural meat chunks in appearance and texture.
  • the product of the invention has the further advantages that this is readily formulated to contain necessary nutrients, is easily digested by the animals and is palatable to the animals.
  • the peptide material in accordance with the invention can also be used for the manufacturing of a nutraceutical or pharmaceutical composition for the prevention and/or treatment of various diseases, as indicated in the claim section.
  • a first aspect of the present invention relates to a peptide prepared from a fish material by a first enzymatic treatment with an alkaline protease and a neutral protease resulting in a fish protein hydrolysate (FPH), and thereafter said fish protein hydrolysate (FPH) is subjected to a second enzymatic treatment with an enzyme preparation manufactured from a strain of Aspergillus oryzae.
  • said enzyme from a strain of Aspergillus oryzae is Umamizyme available from Amano Enzyme Inc., Japan.
  • said alkaline protease and neutral protease is a Bacillus protease complex, preferable ProtamexTM from Novozymes AS.
  • said peptide preparation is substantially fat free.
  • said fish is Salmonidae, preferable Atlantic salmon.
  • said fish is Atlantic salmon
  • the enzyme of the first enzymatic treatment is the Bacillus protease complex ProtamexTM from Novozymes AS and wherein said enzyme from a strain of Aspergillus oryzae is Umamizyme available from Amano Enzyme Inc., Japan, and wherein fat is separated from the peptide material, preferable the first enzymatic treatment.
  • at least 60% of the peptides have a size of 1000 Daltons or less.
  • At least 35% of the peptides have a size of about 100 - 1.000 Dalton, more preferable that at least 40% of the peptides have a size of about 100 - 1.000 Dalton, and more preferable that at about 45% of the peptides have a size of about 100 - 1.000 Dalton.
  • At least 25% of the peptides have a size of less than about 100 Dalton.
  • - at least 35% of the peptides have a size of about 100 - 1.000 Dalton, more preferable that at least 40% of the peptides have a size of about 100 - 1.000 Dalton, and more preferable that at about 45% of the peptides have a size of about 100 - 1.000 Dalton, and
  • - at least 25% of the peptides have a size of less than about 100 Dalton.
  • a fraction of the peptide preparation corresponding to peptide sizes of about 1200 to 200 Daltons has an amino acid composition as indicated in table 4.
  • a fraction of the peptide preparation corresponding to peptide sizes of about 200 to 100 Daltons has an amino acid composition as indicated in table 4.
  • the relative amount of the amino acid arginine in the peptide preparation corresponding to peptide sizes of about 1200 to 200 Daltons is at least 20 %, preferable at least 40 %, more preferable about 60 % lower than compared to the fish protein hydrolysate.
  • the relative amount of the amino acid arginine in the peptide preparation corresponding to peptide sizes of about 200 to 100 Daltons is at least 20 %, preferable at least 40 %, more preferable about 60 % higher than compared to the fish protein hydrolysate.
  • the relative amount of the amino acid tyrosine in the peptide preparation corresponding to peptide sizes of about 1200 to 200 Daltons is 50%, more preferable 100%, more preferable 150 % higher than compared to the fish protein hydrolysate.
  • the peptide preparation can be used for prevention and/or treatment of cardiovascular diseases, wherein said cardiovascular disease preferable is selected from the group consisting of atherosclerosis, angina, cerebrovascular accident (stroke), cerebrovascular disease, congestive heart failure, coronary artery disease, myocardial infarction (heart attack) and peripheral vascular disease.
  • cardiovascular disease preferable is selected from the group consisting of atherosclerosis, angina, cerebrovascular accident (stroke), cerebrovascular disease, congestive heart failure, coronary artery disease, myocardial infarction (heart attack) and peripheral vascular disease.
  • a second aspect of the present invention relates to a process for the preparation of a peptide preparation, characterized in that said preparation is prepared from a fish material by a first enzymatic treatment with an alkaline protease and a neutral protease resulting in a fish protein hydrolysate (FPH), and thereafter said fish protein hydrolysate (FPH) is subjected to a second enzymatic treatment with an enzyme preparation manufactured from a strain of Aspergillus oryzae.
  • said enzyme from a strain of Aspergillus oryzae is Umamizyme available from Amano Enzyme Inc., Japan.
  • said alkaline protease and neutral protease is a Bacillus protease complex, preferable ProtamexTM from Novozymes AS
  • fat is separated from the peptide material after the first enzymatic treatment.
  • said fish is Salmonidae, preferable Atlantic salmon.
  • said treatment is conducted at a pH of about 5 to about 9, preferable at a pH at about 6 to 8, preferable at a pH of about 6 to 7, or more preferable at a pH of about 6.5.
  • a third aspect of the present invention relates to the use of a peptide preparation as a food product or food supplement or nutraceutical preparation for the prevention and/or treatment of cardiovascular diseases, wherein said preparation is prepared from a fish material by a first enzymatic treatment with an alkaline protease and a neutral protease resulting in a fish protein hydrolysate (FPH), and thereafter said fish protein hydrolysate (FPH) is subjected to a second enzymatic treatment with an enzyme preparation manufactured from a strain of Aspergillus oryzae.
  • FPH fish protein hydrolysate
  • a fourth aspect of the present invention relates to the use of a peptide preparation for the manufacturing of a pharmaceutical composition for the prevention and/or treatment of cardiovascular diseases, wherein said preparation is prepared from a fish material by a first enzymatic treatment with an alkaline protease and a neutral protease resulting in a fish protein hydrolysate (FPH), and thereafter said fish protein hydrolysate (FPH) is subjected to a second enzymatic treatment with an enzyme preparation manufactured from a strain of Aspergillus oryzae.
  • FPH fish protein hydrolysate
  • Preferable embodiments of the third and fourth aspect of the present invention relate (independently of each feature and aspect) to;
  • said cardiovascular disease is selected from the group consisting of atherosclerosis, angina, cerebrovascular accident (stroke), cerebrovascular disease, congestive heart failure, coronary artery disease, myocardial infarction (heart attack) and peripheral vascular disease.
  • said cardiovascular disease is treated and/or prevented by increasing the level of high-density lipoprotein (HDL) in the blood.
  • HDL high-density lipoprotein
  • said cardiovascular disease is treated and/or prevented by increasing the ratio of HDL cholesterol to LDL cholesterol in the blood.
  • the use is for the manufacturing of a pharmaceutical or nutraceutical preparation for the prevention and/or treatment of hypocholsterolemia.
  • the use is for the manufacturing of a pharmaceutical or nutraceutical preparation for the prevention and/or treatment of underweight, undernourishment, malnutrition or malnourishment disorders.
  • said disorders are prevented or treated by increasing the body mass index (BMI).
  • BMI body mass index
  • said enzyme from a strain of Aspergillus oryzae is Umamizyme available from Amano Enzyme Inc., Japan.
  • said alkaline protease and neutral protease is a Bacillus protease complex, preferable ProtamexTM from Novozymes AS.
  • said peptide preparation is substantially fat free.
  • a fifth aspect of the present invention relates to a feed composition comprising a peptide preparation in accordance with any of the claims 1 to 16, or prepared by a process in accordance with any of the claims 17-23.
  • said feed composition is for increasing the weight of an animal fed said feed composition.
  • said feed composition is for increasing the weight gain and/or the specific growth rate of an animal.
  • Said animal can be suffering of underweight, undernourishment, malnutrition or malnourishment.
  • mammals include mammals such as humans and farm (agricultural) animals, especially the animals of economic importance such as gallinaceous birds, bovine, ovine caprine and porcine mammals, especially those that produce products suitable for the human consumption, such as meat, eggs and milk.
  • the term is intended to include fish and shellfish, such as salmon, cod, Tilapia, clams and oysters.
  • the term also includes domestic animals such as dogs and cats.
  • treatment refers to a reduction of the severity of the disease, and/or to reduce symptoms of the disease.
  • prevention refers to the preventing of a given disease, i.e. a compound of the present invention is administered prior to the onset of the condition.
  • the compounds of the present invention can be used as prophylactic agents or as ingredients in functional foods or feed in order to prevent the risk or onset of a given disease, or to inhibit deterioration of a given disease.
  • FPH FPH
  • PFH material for the specific fish protein prepared by one enzymatic treatment, i.e. the protein hydrolysate resulting from a primary enzymatic treatment of a fish material with the enzyme mixture ProtamexTM.
  • the Protamex mixture contains an alkaline protease and a neutral protease.
  • the FPH material contains high proportions of proteins and peptides and is used as a control in the experimental section.
  • the peptide material of the present invention is different (due to the second enzymatic treatment) from this FPH material with regard to size distribution of the peptides, and has improved biological activities.
  • the peptide material according to the invention is based on a primary enzymatic treated protein material, and a secondary enzymatic treatment has been conducted in order to reduce the sizes of the peptide fragments.
  • a protease (also termed peptidase or proteinase) breaks down proteins.
  • a protease is any enzyme that conducts proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain forming the protein.
  • Umamizyme available from Amano Enzyme Inc., Japan, has high peptidase activity and high proteinase activity and capable of hydrolyzing various proteins at high level.
  • the materials of the present invention may be administered directly to the animal by any suitable technique, including parenterally, intranasally, orally, or by absorption through the skin. They can be administered locally or systemically.
  • the specific route of administration of each agent will depend, e.g., on the medical history of the animal.
  • the preferred administration route is orally.
  • parenteral administration include subcutaneous, intramuscular, intravenous, intraarterial, and intraperitoneal administration
  • the compounds of the present invention are each typically administered by 1-4 injections per day or by continuous subcutaneous infusions, for example, using a mini-pump.
  • An intravenous bag solution may also be employed.
  • the key factor in selecting an appropriate dose is the result obtained, as measured by decreases in total body weight or ratio of fat to lean mass, or by other criteria for measuring control or prevention of obesity or prevention of obesity-related
  • the compounds of the present invention are formulated generally by mixing each at the desired degree of purity, in a unit dosage injectable form (solution, suspension, or emulsion), with a
  • pharmaceutically acceptable carrier i.e., one that is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation.
  • the formulations are prepared by contacting the compounds of the present invention each uniformly and intimately with liquid carriers or finely divided solid carriers or both. Then, if necessary, the product is shaped into the desired formulation.
  • the carrier is a parenteral carrier, more preferably a solution that is isotonic with the blood of the recipient. Examples of such carrier vehicles include water, saline, Ringer's solution, and dextrose solution. Non-aqueous vehicles such as fixed oils and ethyl oleate are also useful herein, as well as liposomes.
  • the carrier may suitably contain minor amounts of additives such as substances that enhance isotonicity and chemical stability.
  • additives such as substances that enhance isotonicity and chemical stability.
  • Such materials are non-toxic to recipients at the dosages and concentrations employed, and include buffers such as phosphate, citrate, succinate, acetic acid, and other organic acids or their salts; antioxidants such as ascorbic acid; immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids, such as glycine, glutamic acid, aspartic acid, or arginine; monosaccharides, disaccharides, and other carbohydrates including cellulose or its derivatives, glucose, mannose, or dextrins; chelating agents such as EDTA; sugar alcohols such as mannitol or sorbitol; counterions such as sodium; and/or non-ionic surfactants such as polysorbates, poloxamers, or PEG.
  • buffers such as phosphate, citrate
  • compositions such carrier material as, for example, water, gelatine, gums, lactose, starches, magnesium-stearate, talc, oils, polyalkene glycol, petroleum jelly and the like may be used.
  • Such pharmaceutical preparation may be in unit dosage form and may additionally contain other therapeutically valuable substances or conventional pharmaceutical adjuvants such as preservatives, stabilising agents, emulsifiers, buffers and the like.
  • the pharmaceutical preparations may be in conventional liquid forms such as tablets, capsules, dragees, ampoules and the like, in conventional dosage forms, such as dry ampulles, and as
  • the compounds of the present invention are appropriately administered in combination with other treatments for combatting or preventing a specific disease.
  • the invention will be more fully understood by reference to the following examples. They should not, however, be construed as limiting the scope of the invention.
  • a preferred embodiment of the present invention relates to a nutritional composition
  • a nutritional composition comprising the peptide material of the present invention formulated in any conventional way to a feed or food product.
  • Figure 1 shows the control (FPH) and various filtering fractions after treatment with the enzyme preparation Umamizyme as described in example 1.
  • the X-axis shows the logMW for the peptides.
  • Figure 2 shows the effect of the peptide preparation E2 on weight gain relative to control (FPH).
  • Figure 3 shows the effect of the peptide preparation E2 on specific growth rate relative to control (FPH).
  • Figure 4 shows the effect of the peptide preparation E2 on the plasma level of cholesterol relative to control (FPH).
  • Figure 5 shows the effect of the peptide preparation E2 on the plasma level of HDL cholesterol relative to control (FPH).
  • Figure 6 shows the effect of the peptide preparation E2 on the ratio of HDL cholesterol : LDL cholesterol in plasma relative to control.
  • the control material is the enzyme treated fish protein hydrolyzate (FPH) and this material has several beneficial biological effects (as shown in PCT/NO04/00202) .
  • FPH was produced from fish flesh remnants on salmon bone frames after filleting. Frames without heads from freshly filleted Atlantic salmon (Salmo salar, L.) were taken directly from the production line and frozen at -20 ⁇ 2 °C: Within a week the frozen frames were used in the enzymatic hydrolyzing process. The enzymatic hydrolysis was performed with ProtamexTM at a pH of about 6.5 and at temperature of 55 ⁇ 2 °C. ProtamexTM (E.C.
  • 3.4.21.62/3.4.24.28 is a Bacillus protease complex from Novozymes AS (Bagsvaerd, Denmark) containing an alkaline protease and a neutral protease, and fulfils the purity demands for food-grad enzymes.
  • the ratio of salmon frames to water was 1.14.
  • An enzyme to substrate ratio of 1 1.1 AU/kg crude protein was used in the hydrolysis. After 60 min of enzymatic treatment the temperature was elevated to 98 °C, which was reached after 105 min.
  • the evaporated hydrolysate is termed fish protein hydrolyzate (FPH), i.e. the control sample of example 2, and contains about 83 % protein, 10 % ash and about 2 % lipids, based on dry weight.
  • FPH fish protein hydrolyzate
  • the amino acid compositions are given in table 1. Table 1
  • control sample i.e. the hydrolysate obtained by hydro lyses of salmon frames with ProtamexTM.
  • the substrate sample (FPH) (paste) was dissolved in preheated tap water (50 °C) to 10% dry matter.
  • the FPH solution was treated with Umamizyme which is a proteolytic enzyme preparation for protein hydrolysis rich in amino acids.
  • the enzyme preparation is manufactured by a unique fermentation process with a selected strain of Aspergillus oryzae, and is available from Amano Enzyme Inc., Japan.
  • the pH during hydrolysis was 6.5, and the duration was 2.75 hours.
  • the temperature was kept constant at 40 °C. No specific inactivation of the enzymes was carried out after incubation. The inactivation of enzymes was done during the filtration steps and during evaporation of the fractions of interest. In these processing steps the temperature several times exceeded the inactivation temperature of the enzymes included in the study.
  • Figure 1 shows the Peptide distribution of the control sample (FPH) and filtering fractions after treatment with Umamizyme.
  • the peptide distribution was determined as described in the Rubin report no 4617/115, 2004.
  • the enzyme treated solution E2 was refined by Microfiltration and Ultrafiltration in solution with about 10% dry matter at 50 -60 °C.
  • the filtrations were carried out in filtration unit (Membralox SD 3-A modules M-3P1940, Pall, USA) with ceramic membranes with 100 nm and 20 nm pore size (Membralox EP1940, Pall, USA). Only the permeates were collected for evaluation of bioactive peptides, although small samples of the retentates were collected for analytical purposes to have information about yield and performance during the specific filtration steps.
  • the size of the peptides are calculated in accordance with the correlation between elution time and logMW described in the Rubin report 4617/115, 2004.
  • Fig 1 shows the peptide distribution obtained in the various filtering fractions after enzymatic treatment with the enzyme Umamizyme.
  • the secondary enzyme treated preparations (example 2), i.e. the E2 material according to the present invention, and the primary enzyme treated preparation (example 1 ), i.e. the FPH (control), were collected and analysed for total content of amino acids. Only fraction 1 , 2 and 3 were analysed.
  • Fraction 3 26-30 min (corresponding to about 200 - 100 Daltons * Table 3 shows the relative amount of total amino acids detected in the various fractions. Generally the main peptides occurred in Fractions 2 and Fractions 3 for enzymes showing the highest yield in the enzyme hydrolyses.
  • Table 3 show that the secondary enzyme treated (Umamizyme) hydrolysate contain a higher level of amino acids present in smaller peptides (Fraction 2 and fraction 3) as compared to the control (FPH).
  • Table 4 shows the amount of the various amino acids in fraction 2 and 3.
  • the rats will have free access to the intervention diets on day 1-29. All rats are killed on day 30 .
  • DPA docosapentaenoic acid
  • Lipids in whole liver and heparinised plasma were measured in the Tecnicon Axon system (Miles, Tarrytown, NY), with the Bayer triglyceride and cholesterol enzymatic kits (Bayer, Terrytown, NY) and the PAP 150 phospholipid enzymatic kit (bioMerieux, Lyon, France). Liver lipids were first extracted according to Bligh and Dyer (Bligh, E. G. & Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-91. Fatty acid composition
  • Fatty acids were extracted from the samples with 2:1 chloroform: methanol (v/v) (35). The samples were filtered, saponified and esterified in 12% BF 3 in methanol (v/v). Fatty acid composition of total lipids from liver and plasma was analysed using methods described by Lie and Lambertsen (Lie, O. & Lambertsen, G. (1991 ) Fatty acid composition of glycerophospholipids in seven tissues of cod (Gadus morhua), determined by combined high-performance liquid chromatography and gas chromatography. J Chromatogr 565: 1 19-129).
  • Fatty acid methyl esters were separated using a Carlo Erba gas chromatograph ('cold on column' injection, 69°C for 20 s, increase at 25°C min " to 160°C and hold at 160°C for 28 min, increase at 25°C min "1 to 190°C and hold at 190°C for 17 min, increase at 25°C min 1 to 220°C and hold at 220°C for 9 min) equipped with a 50 m CP-sil 88 (Chrompack,
  • the fatty acids were identified by retention time using standard mixtures of methyl esters (Nu- Chek-Prep, Elyian, MN, USA).
  • the fatty acid composition was calculated using an integrator (Turbochrom Navigator, Version 4.0) connected to the GLC.
  • Lipids were extracted from plasma triacylglycerol-rich lipoprotein fraction using a mixture of chloroform and methanol, and separated by thin layer chromatography on silica gel plates (0.25mm Silica gel 60, Merck) developed in hexane-diethyl ether- acetic acid (80:20:1 , v/v/v) and visualized using Rhodamine 6G (0.05% in methanol, Sigma) and UV light. The spots were scraped off and transferred to tubes containing heneicosanoic acid (21 :0) as internal standard. BF 3 -methanol was added to the samples for transesterification.
  • programmable temperature of vaporization injector AS 800 autosampler (Carlo Erba Instrument) and a capillary column (60m x 0.25mm) containing a highly polar SP 2340 phase with film thickness 0.20 ⁇ (Supelco).
  • the initial temperature was 130°C, heating 1 .4°C/min to final temperature 214°C.
  • the injector temperature was 235°C.
  • the detector temperature was 235°C, using hydrogen (25mL/min), air (350 mL/min) and nitrogen as make-up gas (30mL/min). The samples were run with constant flow using hydrogen as a carrier gas (1.6 mL/min). The splitting ratio was 20:1.
  • methyl esters were positively identified by comparison to known standards (Larodan Fine Chemicals, Malmo, Sweden) and verified by mass spectrometry. Quantification of the fatty acids was made with Chrom-Card A/D 1.0 chromatography station (Carlo Erba Instruments) based on heneicosanoic acid as an internal standard.
  • Plasma triacylglycerol-rich lipoprotein fraction was prepared by ultracentrifugation of 3 mL plasma at a density of 1.063 g/mL for 19 hr at 105 000 x g at 15°C. The tubes were sliced, and the floating fraction in the top 1 mL of each tube was harvested. The fraction was then dialyzed against 150 mmol/L sodium chloride, 16 mmol/L sodium phosphate and 4 mmol/L potassium phosphate, pH 7.4, saturated with nitrogen.
  • the E2 material of the present invention increases the weight gain with about 30%. Also the specific growth rate is significantly increased. It is thus anticipated that the E2 material of the present invention can be used as a weight gaining agent, for instance for the prevention or treatment of an underweight, undernourishment disorder or situation, and in feeding regimes for a increasing the weight and/or growth of the fed animals.
  • the initial weight of the rats where (average) 27.3 g and 25.6 g for the control and treatment groups, respectively, and the final weight (after feeding) were 35.1 and 35.6, respectively. This shows that the weight of the E3 fed rats were increased by 2.2 grams (corrected for difference in initial weight) compared to the control group.
  • the peptides of the present invention have thus a general weight increasing effect of about 8.4 %.
  • the peptide material of the present invention increases the level of cholesterol in plasma, and it is thus anticipated that the present invention can be used for the treatment and/or prevention of hypocholsterolemia, i.e. situations with abnormally low levels of cholesterol.
  • High-density lipoprotein (HDL) is one of the five major groups of lipoproteins (chylomicrons, VLDL, IDL, LDL, HDL) that enable lipids like cholesterol and triglycerides to be transported within the water-based bloodstream. In healthy individuals, about thirty percent of blood cholesterol is carried by HDL. It is hypothesized that HDL can remove cholesterol from atheroma within arteries and transport it back to the liver for excretion or re-utilization, which is the main reason why HDL-bound cholesterol is sometimes called "good cholesterol", or HDL-C. A high level of HDL-C seems to protect against cardiovascular diseases.
  • Cardiovascular disease is an abnormal function of the heart or blood vessels. It can cause an increase in risk for heart attack, heart failure, sudden death, stroke and cardiac rhythm problems, thus resulting in decreased quality of life and decreased life expectancy.

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Engineering & Computer Science (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Zoology (AREA)
  • Food Science & Technology (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Health & Medical Sciences (AREA)
  • Nutrition Science (AREA)
  • Organic Chemistry (AREA)
  • Epidemiology (AREA)
  • Mycology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Molecular Biology (AREA)
  • Immunology (AREA)
  • Medicinal Chemistry (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Husbandry (AREA)
  • Animal Behavior & Ethology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • General Engineering & Computer Science (AREA)
  • Genetics & Genomics (AREA)
  • Marine Sciences & Fisheries (AREA)
  • Wood Science & Technology (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Medicinal Preparation (AREA)
  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)

Abstract

La présente invention concerne une préparation peptidique et les procédés pour sa préparation, ainsi que ses utilisations, et une composition alimentaire contenant ladite préparation.
PCT/NO2011/000079 2010-03-08 2011-03-08 Matériau peptidique, composition alimentaire, ses préparations et ses utilisations Ceased WO2011112100A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NO20100370 2010-03-08
NO20100370A NO20100370A1 (no) 2010-03-08 2010-03-08 Peptidmateriale, fôrsammensetninger og preparater, og anvendelser derav.

Publications (2)

Publication Number Publication Date
WO2011112100A1 true WO2011112100A1 (fr) 2011-09-15
WO2011112100A8 WO2011112100A8 (fr) 2012-04-26

Family

ID=44121499

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/NO2011/000079 Ceased WO2011112100A1 (fr) 2010-03-08 2011-03-08 Matériau peptidique, composition alimentaire, ses préparations et ses utilisations

Country Status (2)

Country Link
NO (1) NO20100370A1 (fr)
WO (1) WO2011112100A1 (fr)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2016149956A (ja) * 2015-02-16 2016-08-22 日本ニュートリション株式会社 ほ乳期子豚用発育成績改善剤およびほ乳期子豚育成用配合飼料
US10226422B2 (en) 2013-01-23 2019-03-12 Bottled Science Limited Skin enhancing beverage composition

Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3697285A (en) 1969-10-10 1972-10-10 Rohm & Haas Fish protein solubilization using alkaline bacterial protease
JPH02113859A (ja) 1988-10-24 1990-04-26 Nitto Denko Corp タンパク質加水分解物の製造方法
US4940662A (en) 1982-03-06 1990-07-10 Terumo Kabushiki Kaisha Low-molecular weight peptide mixture and method of producing same
WO1994025580A1 (fr) 1993-04-26 1994-11-10 Novo Nordisk A/S Procede d'hydrolyse de proteines
WO2005002605A1 (fr) * 2003-07-04 2005-01-13 Thia Medica As Hydrolysat proteique de poisson
WO2006005757A2 (fr) 2004-07-12 2006-01-19 Dsm Ip Assets B.V. Hydrolysats proteiques abaissant la pression sanguine
WO2006084383A1 (fr) * 2005-02-14 2006-08-17 Ocean Nutrition Canada Limited Supplement dietetique antidiabetique et antihypertensif
WO2006084351A1 (fr) 2005-02-14 2006-08-17 Ocean Nutrition Canada Limited Complement dietetique anti-hypertensif derive d'hydrolysats de proteines de saumon ou d'oncorhynchus
FR2927335A1 (fr) * 2008-02-12 2009-08-14 Cie Des Peches Saint Malo Sant Hydrolysat de proteines de poissons presentant une activite satietogene, compositions nutraceutiques et pharmacologiques comprenant un tel hydrolysat et procede d'obtention
WO2009128713A1 (fr) 2008-04-14 2009-10-22 Newtricious B.V. Hydrolysats de protéine d'œuf

Patent Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3697285A (en) 1969-10-10 1972-10-10 Rohm & Haas Fish protein solubilization using alkaline bacterial protease
US4940662A (en) 1982-03-06 1990-07-10 Terumo Kabushiki Kaisha Low-molecular weight peptide mixture and method of producing same
JPH02113859A (ja) 1988-10-24 1990-04-26 Nitto Denko Corp タンパク質加水分解物の製造方法
WO1994025580A1 (fr) 1993-04-26 1994-11-10 Novo Nordisk A/S Procede d'hydrolyse de proteines
WO2005002605A1 (fr) * 2003-07-04 2005-01-13 Thia Medica As Hydrolysat proteique de poisson
WO2006005757A2 (fr) 2004-07-12 2006-01-19 Dsm Ip Assets B.V. Hydrolysats proteiques abaissant la pression sanguine
WO2006084383A1 (fr) * 2005-02-14 2006-08-17 Ocean Nutrition Canada Limited Supplement dietetique antidiabetique et antihypertensif
WO2006084351A1 (fr) 2005-02-14 2006-08-17 Ocean Nutrition Canada Limited Complement dietetique anti-hypertensif derive d'hydrolysats de proteines de saumon ou d'oncorhynchus
FR2927335A1 (fr) * 2008-02-12 2009-08-14 Cie Des Peches Saint Malo Sant Hydrolysat de proteines de poissons presentant une activite satietogene, compositions nutraceutiques et pharmacologiques comprenant un tel hydrolysat et procede d'obtention
WO2009128713A1 (fr) 2008-04-14 2009-10-22 Newtricious B.V. Hydrolysats de protéine d'œuf

Non-Patent Citations (7)

* Cited by examiner, † Cited by third party
Title
BERGE, R. K., FLATMARK, T., OSMUNDSEN, H.: "Enhancement of long-chain acyl-CoA hydrolase activity in peroxisomes and mitochondria of rat liver by peroxisomal proliferators", EUR J BIOCHEM, vol. 141, 1984, pages 637 - 644
BLIGH, E. G., DYER, W. J.: "A rapid method of total lipid extraction and purification", CAN J BIOCHEM PHYSIOL, vol. 37, 1959, pages 911 - 91
COHEN, MICHAUD, ANAL. BIOCHEM., vol. 211, 1993, pages 279 - 287
GUERARD F ET AL: "Production of tuna waste hydrolysates by a commercial neutral protease preparation", JOURNAL OF MOLECULAR CATALYSIS. B, ENZYMATIC, ELSEVIER, AMSTERDAM, NL, no. 19-20, 2 December 2002 (2002-12-02), pages 489 - 498, XP002293270, ISSN: 1381-1177, DOI: DOI:10.1016/S1381-1177(02)00203-5 *
LAURA GILMARITN ET AL.: "Production of Cod (Gadus morhua) Muscle Hydrolysates, Influence of Combinations of Commercial Enzyme Preparations on Hydrolysate Peptide Size Range", J. AGRIC. FOOD CHEM., vol. 50, 2002, pages 5417 - 5423
LIE, O., LAMBERTSEN, G.: "Fatty acid composition of glycerophospholipids in seven tissues of cod (Gadus morhua), determined by combined high-performance liquid chromatography and gas chromatography", J CHROMATOGR, vol. 565, 1991, pages 119 - 129
WERGEDAHL HEGE ET AL: "Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA:Cholesterol acyltransferase activity in liver of Zucker rats", JOURNAL OF NUTRITION, vol. 134, no. 6, June 2004 (2004-06-01), pages 1320 - 1327, XP002641826, ISSN: 0022-3166 *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US10226422B2 (en) 2013-01-23 2019-03-12 Bottled Science Limited Skin enhancing beverage composition
JP2016149956A (ja) * 2015-02-16 2016-08-22 日本ニュートリション株式会社 ほ乳期子豚用発育成績改善剤およびほ乳期子豚育成用配合飼料

Also Published As

Publication number Publication date
NO20100370A1 (no) 2011-09-09
WO2011112100A8 (fr) 2012-04-26

Similar Documents

Publication Publication Date Title
US8206739B2 (en) Fish protein hydrolyzate
Erdmann et al. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
Khora Marine fish-derived bioactive peptides and proteins for human therapeutics
Xing et al. Marine products as a promising resource of bioactive peptides: Update of extraction strategies and their physiological regulatory effects
WO2007080515A1 (fr) Extrait de krill prevenant la thrombose
Zhang et al. Extraction, bioactive function and application of wheat germ protein/peptides: A review
WO2011112099A1 (fr) Matériau peptidique, ses préparations et ses utilisations
CN117143949A (zh) 一种南极磷虾源高f值寡肽及其在护肝中的应用
WO2011112100A1 (fr) Matériau peptidique, composition alimentaire, ses préparations et ses utilisations
JP3787585B2 (ja) アンジオテンシン変換酵素阻害物質、その製造方法およびそれを用いた血圧降下剤
WO2011112101A1 (fr) Matériau peptidique, composition alimentaire, ses préparations et ses utilisations
US20070141083A1 (en) Use of a single-cell protein material
CN113444759A (zh) 一种乙醇脱氢酶激活肽及其制备方法
EP0680757B1 (fr) Utilisation de principes actifs protégés vis-à-vis de la dégradation dans le rumen comme hépatoprotecteurs
WO2010131718A1 (fr) Agent anti-hyperglycémique et/ou anti-hyperlipidémique comprenant une matière contenant de la sphingomyéline issue de la peau d'oiseau comme ingrédient actif
JP5893236B2 (ja) 生体コラーゲン合成促進剤
Sethuramalingam et al. Anti-oxidant, anti-inflammatory and anti-atherosclerotic activity of bioactive peptide HPAEDR isolated from Catla catal muscle on LPS induced inflammation on 246.7 raw macrophage cells and HCF induced hyperlipidemic Zebrafish Larvae
JP6418579B2 (ja) ホタテ貝外套膜のタンパク質分解物を有効成分とする脂質吸収促進剤及びこれを含む飲食品
Hernández-Corroto et al. Bioactive peptides from fruit food waste after simulated gastrointestinal digestion
KR20030015537A (ko) 혈중 지질 농도 저하용 펩타이드의 제조 방법
Abachi-Hokmabadinazhad Characterization and identification of hypotensive, immunomodulatory, and metabolic disorder benefiting peptides from Atlantic mackerel (Scomber scombrus) hydrolysate separated based on molecular weight, charge, and hydrophobicity
CN120795074A (zh) 缓解卵巢衰退的海参卵肽及其制备方法和应用
Park et al. Cholesterol lowering effect of enzymatic hydrolysates of squid in rats
JPH05339168A (ja) 膵リパーゼおよびコレステロールエステラーゼ阻害剤
CN114106125A (zh) 一种银杏肽和含所述银杏肽的特殊医学用配方食品及应用

Legal Events

Date Code Title Description
DPE2 Request for preliminary examination filed before expiration of 19th month from priority date (pct application filed from 20040101)
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 11714863

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 11714863

Country of ref document: EP

Kind code of ref document: A1