EP3197288A1 - Isolement d'oligopeptides végétaux et leurs utilisations - Google Patents

Isolement d'oligopeptides végétaux et leurs utilisations

Info

Publication number
EP3197288A1
EP3197288A1 EP15822094.7A EP15822094A EP3197288A1 EP 3197288 A1 EP3197288 A1 EP 3197288A1 EP 15822094 A EP15822094 A EP 15822094A EP 3197288 A1 EP3197288 A1 EP 3197288A1
Authority
EP
European Patent Office
Prior art keywords
isolate
retentate
daltons
filtrate
molecular weight
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.)
Withdrawn
Application number
EP15822094.7A
Other languages
German (de)
English (en)
Other versions
EP3197288A4 (fr
Inventor
Xinqi Liu
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.)
Individual
Original Assignee
Individual
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 Individual filed Critical Individual
Publication of EP3197288A1 publication Critical patent/EP3197288A1/fr
Publication of EP3197288A4 publication Critical patent/EP3197288A4/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • 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
    • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
    • A23L2/52—Adding ingredients
    • 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
    • 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
    • A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
    • 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
    • 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
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • 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
    • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
    • 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
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14—Extraction; Separation; Purification
    • C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2200/00—Function of food ingredients

Definitions

  • the present invention generally relates to plant and marine protein oligopeptide enriched isolates and deep processing for producing the same. More particularly, the present invention relates to a high- yield method of isolating a granular, free-flowing, non-dusting, low molecular weight oligopeptides with improved suitability for incorporation into industrial applications.
  • peptide isolates may include substance obtained by acidic, alkaline or enzymatic hydrolysis of protein composed primarily of amino acids, peptides and proteins and may contain impurities consisting chiefly of carbohydrates and lipids along with smaller quantities of miscellaneous organic substances of biological origin.
  • Peptide isolates have documented applications in textiles including applications such as plywood adhesives; aquaculture and agriculture including applications such as promotion of plant rooting, germination, growth and prolong lifetime; biofuels; cosmetic formulation; biopharmaceuticals and absorbent hydrogel formulation; functional food and beverage formulation; enteric diet formulation and dietary supplementation; infant and pediatric nutritional product formulation; animal feed formulation; cell culture growth medium and fermentation processing; baking ingredient to improve resistance against freezing and favorable texture.
  • bioactive peptides as antioxidants, anticoagulants, anti-inflammatory modulators, antibacterial, antifungal and antiviral agents, thermogenic agents, anticancer (colon and prostate), anti-osteoporosis, cell growth and repair modulators, angiotensin-converting enzyme (ACE) inhibitors, in addition to biological signaling mediators involved in a myriad of signaling functions with impact on recovery, lipid metabolism, carbohydrate metabolism, immune function, cardiovascular and bone health, nervous system and brain function, optimizing muscle performance during exercise, digestive satiety and weight management.
  • ACE angiotensin-converting enzyme
  • the invention discloses a high-yield method for processing plant and marine protein isolates to produce a uniform, granular, low -molecular weight oligopeptide enriched isolate with a narrow molecular weight distribution obtained by a novel functional sequence of ultra-high temperature processing treatment prior to enzymatic hydrolysis, dilution ratio and Brix parameters for hydrolysis and separation, nanofiltration, coupled fluidized bed and spray drying followed by drum drying.
  • the present invention has accounted for the aforementioned circumstances and embodies enrichment of protein isolates to improve product purity and stability and provide strict control of the product molecular weight range.
  • the object of the present invention is to provide means useful for establishing a superior oligopeptide isolate production system for plant and marine -derived protein isolates.
  • the comestible composition may include but is not limited to, a tablet, food, candy, gel, powder, beverages selected from carbonated water, flavored water, carbonated flavored water, spring water, fruit juice, vegetable juice or nectar, coffee, decaffeinated coffee, tea, fruits and products derived from tea, herbal products from tea, decaffeinated tea, wine, champagne, ale , rum, gin, vodka, other liquor, milk obtained from animals, from soybeans, rice, coconut milk or other plant products.
  • Beverage selected from the group consist of, but are not limited to sports beverages, beverage concentrates, hypotonic beverages, soft drinks, strong drinks (shot), sport drinks, hypertonic drinks, energy drinks and isotonic drinks.
  • Nutritional formulations optionally comprises one or more amino acids, antioxidants, fat, vitamins, trace elements, electrolytes, sweeteners, flavors and / or mixtures thereof, caffeine, coloring agents, emulsifying agents, flavor enhancers, food grade acids, minerals, micronutrients, botanical extracts, phytochemicals, preservatives, buffer salts include salts class, stabilizers, thickeners, pharmaceutical ingredients, fiber, prebiotics, probiotics and / or combinations thereof.
  • the present invention is a concentrated oligopeptide isolate derived from plant or marine protein isolates comprising a higher total proportion of narrowly distributed, low molecular weight peptides with a lower total proportion of free amino acids in a free-flowing, uniform granules of 40 to 60 ⁇ particle size with a low moisture content and soluble hydrate at low pH with a method of producing the same comprising ultra-high temperature processing treatment from 130 to 150°C, hydrolysis under conditions of 5 to 20°Bx, separation Brix parameters of 4 to 20°Bx, 1 to 15 ratio water wash after microfiltration, nanofiltration by pulsating flow pressure at 10 to 35°Bx, coupled fluidized bed and spray drying followed by drum drying to form a concentrated granular oligopeptide isolate.
  • the present invention it is possible to achieve plant or marine protein oligopeptide enriched isolates in high-yield with fluidity, dispersion, solubility, sensory properties and interaction stability are consistent and well-suited for industrial applications.
  • the hydrate remains clear under acidic and low temperature conditions and the viscosity of the hydrate is low.
  • the product is stable, potent and easily absorbed by the body.
  • the scope of the present invention can be widely used in the form and added as the form to include, but not limited to applications in pharmaceutical, preventative health, dietary supplement, functional food and beverage, pediatric nutrition, food additive, animal feed, fertilizer, antioxidant, antimicrobial, cosmetic, surfactant, adhesive and bio-fuel formulations.
  • the oligopeptide enriched isolate described in the present invention can also be fermented with different types of starter or probiotic cultures or can be combined with all kinds of ingredients such as oils, fats, emulsifiers, carbohydrates, fruit concentrates, flavors, colorants, alcohol, carbon dioxide, thickeners, acidulates, antioxidants, herbs or herb extracts, health promoting compounds like vitamins or bioactive compounds formulate a product which is in line with the marketing needs.
  • ingredients such as oils, fats, emulsifiers, carbohydrates, fruit concentrates, flavors, colorants, alcohol, carbon dioxide, thickeners, acidulates, antioxidants, herbs or herb extracts, health promoting compounds like vitamins or bioactive compounds formulate a product which is in line with the marketing needs.
  • a peptide or oligopeptide are defined as a chain of at least two amino acids that are linked through peptide bonds.
  • the terms "peptide” and “oligopeptide” can be used interchangeably as the context requires.
  • a protein consists of one or more chain comprising of more than 30 amino acid residues (polypeptides) linked together by peptide bonds.
  • a protein hydrolysate, hydrolysate, or hydrolysed protein is the product that is formed by hydrolysis of the protein peptide bonds between amino acids.
  • An enriched hydrolysate being a fraction of the protein hydrolysate, for example enriched in selected peptides or wherein a subset of peptides or polypeptides have been removed from the hydrolysate. So an enriched hydrolysate is preferably a mixture of peptides or a peptide mixture.
  • Raw materials may include legume, seed, grain, marine and other sprouted or un-sprouted plant protein isolates.
  • raw plant and marine proteins include, but are not limited to, protein and polypeptides derived from soybean, pea, corn, canola, Jatropha, palm, peanut, sunflower, coconut, mustard, cotton seed, Palm kernel, olive, safflower, sesame, linseed and microbial proteins or polypeptides from yeast or bacterium.
  • whole plant or marine protein isolates may be standard, commoditized plant or marine protein isolates.
  • the protein source may be whole or any product or by-product derived from the processing of plant or marine protein sources including but not limited to meal, flakes, grits and flour.
  • the protein source may be used in the full fat form, partially defatted form or fully defatted form. Where the protein source contains an appreciable amount of fat, an oil-removal step is generally required during the process.
  • the protein recovered from the protein source may be the protein naturally occurring in in plant or marine sources or the proteinaceous material may be a protein modified by genetic manipulation but possessing characteristic hydrophobic and polar properties of the natural protein.
  • Protein isolation can be performed by any method know in the art. The general, conventional procedures for protein isolates of various plant or marine origin are described in the prior art. Typically, processing will include isolation of the protein containing portion of the organism, flaking, extraction of fat and decanting insoluble materials, such as fiber and cellulose, followed by pH adjustments. Where the protein isolate starting material contains an appreciable amount of unmodified protein materials, purification of protein isolate may be required before proceeding with the embodiment of the present invention. Specifically, an antecedent protein concentration or separation via hydrolysis may be required and can also be further purified by activated carbon or adsorbent resin. Preferably a starting protein isolate material is comprised of more than 50% (w/w) protein, more preferably 90% (w/w) protein.
  • Protein isolates are used as the starting material, the embodiment of the present invention encompasses the isolation and concentration of low -molecular-weight oligopeptides for industrial applications from the starting material.
  • the alkaline solution comprises an alkaline material of sodium hydroxide, calcium hydroxide, magnesium hydroxide, potassium hydroxide or mixtures thereof. More preferably, the alkaline solution comprises sodium hydroxide.
  • [0020] Maintain the solution temperature at 40 to 70°C and the Brix at 5 to 20°Bx by adjusting with a non-reducing sugar.
  • non-reducing sugars include, but are not limited to raffinose, stachyose, sucrose and verbascose.
  • Hydrolyzing agent for use in the processes of the present invention may include enzymes, including proteases. The hydrolysis is preferably carried out by protease treatment.
  • protease animal origin, plant origin or microbial origin can be appropriately selected based on the raw material protein source.
  • Suitable proteases may include: metalloendoproteases such as bacillolysin, Neutrase®, Maxazyme N P DS®; serine endoprotease such as trypsin, chymotrypsin, subtilisin (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo subtilisin A, subtilopeptidase A, alcalase Novo, similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species and commercially available under names Alcalase ® or Protex®) Streptomyces alkaline protease, Bioplase®, Protease P®; cystein endopeptidase such as papain or bromelain
  • the hydrolyzing agent is Alcalase®.
  • Reaction pH, reaction temperature of the protease treatment may be altered to suit the characteristics of the protease used, but generally it is possible to carry out the reaction at a pH between 6 and 8 and temperature 40 to 70°C.
  • the degree of hydrolysis is the extent to which peptide bonds are broken by the enzymatic hydrolysis reaction. The degree of hydrolysis most preferably between 10 and 50%.
  • Ultra-high temperature process sterilize the retentate at 130 to 150°C for 15 to 60 seconds.
  • Spray dry the retentate Preferably, with built-in fluidized bed tower. More preferably, maintain the inlet temperature at 140 to 180°C, bed temperature at 60 to 100°C, exhaust temperature at 90 to 110°C and pressure at -20 to -80 Pa.
  • Material proportions may be adjusted as scale demands. Likewise, system conditions may be adjusted. Brix may be adjusted by alternative soluble solids. Molecular weight cut-off may be adjusted to meet specific application requirements. The step described herein the best mode can be performed in the same manner for plant or marine protein isolates to produce the oligopeptide concentrated isolate according to the present invention described above.
  • Proteins make up all of the body's organs and are required for proper function of organ systems. All proteins are made up of amino acids, but differences in amino acid composition and sequence differentiate how proteins function. The body uses amino acids to construct specific proteins for specific functions in the maintenance of organ health. However, the body has no de novo route for synthesis of many necessary amino acids, therefore these essential amino acids must be obtained from dietary protein. The body must consistently digest, absorb and metabolize adequate dietary proteins to supply organs with the specific proteins needed to function. Several other challenges exist. Complete dietary proteins often come from animal sources and are accompanied by cholesterol, which can be a rate-limiting factor for dietary consumption. As the body ages, digestive function tends to decline resulting in inefficient absorption of large dietary proteins. Another difficulty is that absorbed dietary proteins are not stored by the body to be metabolized later, so if all amino acids necessary to construct specific proteins are not present in optimal ratios during the metabolism, protein synthesis is inefficient
  • Protein isolate supplements can effectively supply proteins to the body "just-in-time.” Cholesterol can be eliminated by isolating proteins from complete, vegetarian sources. Dietary protein can be more easily digested and absorbed by consuming smaller peptide subunits of proteins. Protein synthesis can be made more efficient by consuming dietary protein with optimized amino acid balance.
  • the current invention offers a solution for achieving plant peptide concentrates in high-yield with physical, chemical and biological attributes suitable for industrial applications.
  • the scope of the invention includes, but is not limited to applications in pharmaceutical, preventative health, dietary supplement, functional food and beverage, pediatric nutrition, food additive, animal feed, fertilizer, antioxidant, antimicrobial, cosmetic, surfactant, adhesive and bio-fuel formulations.
  • Protein isolate was dissolved in various ratios of water after microfiltration (g) and processed similarly through steps (h) to (k). Yield was measured as total yield of isolation over total starting raw material
  • Protein isolate was maintained at various Brix concentration after microfiltration (g) and processed similarly through steps (h) to (k). Yield was measured as total yield of isolation over total starting raw material (w/w).
  • Protein isolate was maintained at various Brix concentration after microfiltration (h) and processed similarly through steps (i) to (i).
  • Optical density (OD) measurements were taken at 660 nm to measure fluid clarity before drying.
  • Protein isolate was processed similarly through steps (a) to (k), where steps (f) to (g) were compared to conventional centrifugation separation methods. Yield was measured as total yield of isolation over total starting raw material (w/w).
  • Protein isolate was processed similarly through steps (a) to (k), where steps (f) to (g) were compared to conventional centrifugation separation methods.
  • Optical density (OD) measurements were taken at 660 nm to measure fluid clarity before drying.
  • Soy protein isolate was chosen as the raw starting material wherein yielding protein content is comprised of about 95% oligopeptides.
  • the isolated protein content molecular weight distribution was assessed on multiple batch preparations using the methods disclosed in this invention. A conventional isolation method by centrifugation and commercial soy peptide products were also assessed for comparison. Measurement of protein content, with respect to the dry weight of the various isolated protein material. The weight of the crude protein mass was measured by the Kjeldahl method, it expressed in weight percent. In addition, nitrogen coefficient it was 6.25.
  • the molecular weight distribution of soy protein fraction of the hydrolyzate it was measured by HPLC method using the following gel filtration column.
  • the set an HPLC system using a gel filtration column for peptide was charged with a known peptide comprising a molecular weight marker, to determine the calibration curve at the retention time of the relationship between the molecular weight.
  • the isolate was diluted two -fold with gel filtration solvent (1% SDS in lOmM phosphate buffer, pH 8.0) and 5 ⁇ L was applied it to the HPLC column (GE Healthcare Superdex Peptide 7.5 300GL).
  • the column temperature was 25°C, flow rate 0.25 mL per minute and detection wavelength 220 nm.
  • the percentage of molecular weight to the total amount of peptides and free amino acids in the isolate were calculated for the area of the entire absorbance in the time range.
  • the isolated product was reconstituted in 1 : 10 in water (w/v). pH (adjusted to the appropriate level with diluted NaOH or HCI) and temperature were adjusted and solution clarity was assessed by optical density (OD) measurements at 610 nm on multiple batch preparations using the methods disclosed in this invention. A lower absorbance score indicates greater clarity. Solubility was assessed as the protein content of the dispersions, measured by nitrogen determination. 10 mL aliquots were transferred to pre-weighed centrifuge tubes and centrifuged at 7,800 g for 10 minutes to sedimented the insoluble material. The protein content of the supernatant was measured by nitrogen content. The pellet material was dried overnight in an oven set at 100° C and the weight of dry pellet material was recorded.
  • Solubility (%) was calculated by (% protein in supernatant/% protein in initial dispersion) xlOO.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Polymers & Plastics (AREA)
  • Food Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Nutrition Science (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Organic Chemistry (AREA)
  • Molecular Biology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Zoology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biophysics (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Analytical Chemistry (AREA)
  • Water Supply & Treatment (AREA)
  • Animal Husbandry (AREA)
  • Mycology (AREA)
  • Marine Sciences & Fisheries (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Peptides Or Proteins (AREA)

Abstract

L'invention concerne un isolat enrichi en oligopeptides granulaire, fluide, ne produisant pas de poussière, à distribution étroite des faibles poids moléculaire, dérivé d'isolats de protéines de légumineuses, de semences, de grains, de plantes marines et autres germées et non germées et qui convient mieux à des applications industrielles et un procédé pour le préparer. Le nouvel isolat d'oligopeptides présente une fluidité, une dispersion, une solubilité, des propriétés sensorielles, une stabilité et une sécurité vis-à-vis des interactions et une innocuité constantes et bien adaptées pour des applications. La viscosité et la clarté de l'hydrate sont bien adaptées pour des applications. Le produit est stable, efficace et facilement absorbé par l'organisme. Le procédé efficace de traitement utilisé pour produire l'isolat d'oligopeptides comprend un traitement de transformation à ultra-haute température avant une hydrolyse enzymatique, un rapport de dilution et paramètres Brix pour l'hydrolyse et la séparation, la nanofiltration et le séchage sur lit fluidisé et par pulvérisation couplés, puis un procédé de séchage en tambour. L'isolat enrichi en oligopeptides végétaux ou marins obtenu convient non seulement à l'enrichissement nutritionnel de milieux acides, mais peut également être utilisé dans des applications classiques très diverses d'isolats de protéines, notamment mais pas exclusivement, l'enrichissement d'aliments et de boissons acides et non acides, l'émulsification d'huiles, en tant qu'agent de formation de corps dans des produits de boulangerie ou agent moussant dans des produits qui piègent des gaz, dans des formulations pharmaceutiques, de prévention en matière de santé, de complément alimentaire, de nutrition pédiatrique, d'additif alimentaire, d'aliment pour animaux de compagnie ou d'élevage, d'engrais, d'antioxydant, antimicrobiennes, cosmétiques, tensioactives, adhésives et de biocarburant.
EP15822094.7A 2015-07-15 2015-07-15 Isolement d'oligopeptides végétaux et leurs utilisations Withdrawn EP3197288A4 (fr)

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
PCT/IB2015/055341 WO2016009364A1 (fr) 2014-07-14 2015-07-15 Isolement d'oligopeptides végétaux et leurs utilisations

Publications (2)

Publication Number Publication Date
EP3197288A1 true EP3197288A1 (fr) 2017-08-02
EP3197288A4 EP3197288A4 (fr) 2018-05-16

Family

ID=61131857

Family Applications (1)

Application Number Title Priority Date Filing Date
EP15822094.7A Withdrawn EP3197288A4 (fr) 2015-07-15 2015-07-15 Isolement d'oligopeptides végétaux et leurs utilisations

Country Status (2)

Country Link
EP (1) EP3197288A4 (fr)
WO (1) WO2016009364A1 (fr)

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US11102998B1 (en) 2017-08-25 2021-08-31 The Hershey Company Binders and methods of making and using the same
CN108783467B (zh) * 2018-06-04 2021-08-06 中食月太(北京)健康科技有限公司 改善骨质疏松和增加骨密度的组合物及其制备方法
CN111088049B (zh) * 2019-12-06 2021-06-01 湖南鑫利生物科技有限公司 一种制备迷迭香脂溶性抗氧化剂油膏的方法
CN119371253B (zh) * 2024-12-31 2025-03-25 山东鲁花地生生物科技有限公司 一种含植物蛋白肽功能性肥料的制备方法及应用

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4443540A (en) * 1980-05-09 1984-04-17 University Of Illinois Foundation Protein hydrolysis
US5691165A (en) * 1991-05-31 1997-11-25 Novo Nordisk A/S Method for production of a whey protein hydrolyzate
DE60332024D1 (de) * 2002-08-05 2010-05-20 Fuji Oil Co Ltd Verfahren zur herstellung von soja protein
NO320964B1 (no) * 2004-05-26 2006-02-20 Norcape Biotechnology As Hydrolysert marint proteinprodukt og et fôrprodukt omfattende dette, fremgangsmate for fremstilling og anvendelse
CN100589702C (zh) * 2005-09-20 2010-02-17 中国食品发酵工业研究院 一种高纯度、低分子量的大豆低聚肽粉的工业生产方法
CN101319245A (zh) * 2008-07-16 2008-12-10 青岛柯能生物科技有限公司 鱼胶原蛋白肽纳滤分子量分级技术
CN101824455B (zh) * 2009-03-06 2013-07-17 香港百特有限公司 一种大豆蛋白低聚肽及其制备方法和用途

Also Published As

Publication number Publication date
WO2016009364A1 (fr) 2016-01-21
EP3197288A4 (fr) 2018-05-16

Similar Documents

Publication Publication Date Title
JP7121059B2 (ja) ジケトピペラジンを含有する植物エキス及びその製造方法
Feng et al. Effect of solid-state fermentation on plant-sourced proteins: A review
US20220024974A1 (en) Methods for producing a rice protein peptide and applications thereof
US9609883B2 (en) Method for producing wheat glutamine peptide
CN101558791A (zh) 一种基于双蛋白的多肽豆奶粉及其制备方法
CN101787387B (zh) 一种耐酸和无苦味的大豆寡肽及其生产方法与应用
CN102080118A (zh) 一种米糠抗氧化活性蛋白肽的制作
US20170156369A1 (en) Isolation of Plant Oligopeptides and Uses Thereof
CN102138627B (zh) 一种植物源呈味肽及其制备方法
EP3197288A1 (fr) Isolement d'oligopeptides végétaux et leurs utilisations
CN103045705A (zh) 一种由鱼蛋白肽与大豆肽组成的蛋白肽的生产方法
Cesaretti et al. Protein hydrolysates: from agricultural waste biomasses to high added-value products (minireview)
CN101717763B (zh) 一种提高液体氨肽酶稳定性的方法及该酶的应用
US20100286034A1 (en) Uses for aqueous streams containing proteins
KR20220055645A (ko) 매우 낮은 분자량의 어류 유래 콜라겐 펩타이드의 제조 방법
JP2006296213A (ja) アスパラガスより得られる組成物
KR100503100B1 (ko) 쌀겨로부터 식물성 단백질 분해효소를 이용하여 저 분자화 된 펩타이드를 간단히 제조하는 방법
Jauregi et al. Enzymatic processes for the production of food ingredients from food processing by-products
Handayani et al. Chemical characteristics and activity of ACE inhibitors on fractionation of tempeh koro kratok (Phaseolus lunatus) peptides
JP2006111583A (ja) γ−アミノ酪酸含有組成物及びその製造方法
Lobo et al. Ingredients of high nutritional value obtained from Latin-American crops through biotechnology
JPH05161473A (ja) 栄養補助食品
JP6477710B2 (ja) メナキノン−７含有培養物及びメナキノン−７の製造法
KR100578495B1 (ko) 청국장을 이용한 발효 두유의 제조방법
KR20220159195A (ko) 천연 아미노산 분말의 제조방법

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20170410

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR

AX Request for extension of the european patent

Extension state: BA ME

DAV Request for validation of the european patent (deleted)
DAX Request for extension of the european patent (deleted)
A4 Supplementary search report drawn up and despatched

Effective date: 20180413

RIC1 Information provided on ipc code assigned before grant

Ipc: C07K 1/02 20060101ALI20180409BHEP

Ipc: A23J 3/30 20060101AFI20180409BHEP

Ipc: A23J 3/34 20060101ALI20180409BHEP

17Q First examination report despatched

Effective date: 20180525

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: THE APPLICATION IS DEEMED TO BE WITHDRAWN

18D Application deemed to be withdrawn

Effective date: 20181005