WO2002045522A1 - Isolement de glycomacropeptides de caseine a partir de lactoserum par chauffage et denaturation minimale des glycomacropeptides de caseine - Google Patents

Isolement de glycomacropeptides de caseine a partir de lactoserum par chauffage et denaturation minimale des glycomacropeptides de caseine Download PDF

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Publication number
WO2002045522A1
WO2002045522A1 PCT/NZ2001/000265 NZ0100265W WO0245522A1 WO 2002045522 A1 WO2002045522 A1 WO 2002045522A1 NZ 0100265 W NZ0100265 W NZ 0100265W WO 0245522 A1 WO0245522 A1 WO 0245522A1
Authority
WO
WIPO (PCT)
Prior art keywords
whey protein
inclusive
casein
source
range
Prior art date
Application number
PCT/NZ2001/000265
Other languages
English (en)
Inventor
Rex Stuart Humphrey
Janine Lee Broekhuizen
Faydra Ann Sievers
Original Assignee
Tatua Co-Operative Dairy Company Limited
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 Tatua Co-Operative Dairy Company Limited filed Critical Tatua Co-Operative Dairy Company Limited
Priority to AU2002216479A priority Critical patent/AU2002216479A1/en
Publication of WO2002045522A1 publication Critical patent/WO2002045522A1/fr

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Classifications

    • 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
    • A23J3/343—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy 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
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/20—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from milk, e.g. casein; from whey
    • A23J1/205—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from milk, e.g. casein; from whey from whey, e.g. lactalbumine
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4732—Casein

Definitions

  • the present invention is directed to the isolation of protein rich products from a whey protein source.
  • Whey protein concentrates and isolates are commercially available products produced in the dairy industry. They are by-products of a number of dairy manufacturing processes including the manufacture of cheese and rennet casein.
  • compositions of these whey protein products vary depending upon a number of 10 factors including the manufacturing processes of which they are by-products, as well as other geographical and seasonal variations.
  • whey protein products have some value due to their high protein content. Some are also more valuable because of their specific protein composition. Their value can be substantially increased by fractionation of specific proteins from the 15 product mixture.
  • the proteins which are commercially more valuable as fractions include casein glycomacropeptides (GMP), ⁇ -lactalbumin, ⁇ -lactoglobulin, and proteins which can be transformed into whey protein hydrolysates.
  • GMP casein glycomacropeptides
  • ⁇ -lactalbumin ⁇ -lactalbumin
  • ⁇ -lactoglobulin proteins which can be transformed into whey protein hydrolysates.
  • the first supernatant is then concentrated by ultrafiltration, leading to a retentate which is then treated with ethanol to produce a precipitate and a second supernatant.
  • the second supernatant can be collected by a second ultrafiltration step and dried.
  • WO 99/29183 itself discloses an alternative process of isolating casein glycomarcopeptide (GMP), wherein the whey protein source is acidified to below pH 4.0 and the solution treated by cold ultrafiltration at around 12 °C before readjusting the pH of the solution to pH 6.7 and subjecting to another cold ultrafiltration step.
  • GMP glycomarcopeptide
  • EP 0,488,589 Another method of GMP isolation is disclosed by EP 0,488,589 which involves contacting raw milk materials containing GMP with an ion-exchanger, collecting the fraction which does not absorb to the resin and treating this solution to obtain GMP. This process also does not involve heat denaturation steps as per the subject invention.
  • Heat denaturation of the whey protein source is also known in the art, being a much simpler and more cost-effective way of industrially isolating GMP. It is essential
  • WO 94/15952 discloses a process for the isolation of GMP involving of a heat treatment step to denature the whey protein followed by acidifying the solution to pH 4-5 to precipitate the whey proteins whilst keeping the GMP in solution, which can then be collected by ultrafiltration.
  • a step in a method for the separation of casein glycomacropeptides from a whey protein source said step being
  • casein glycomacropeptide should be taken to mean the macropeptide from ⁇ -casein X(fl06-169).
  • GMP casein glycomacropeptide
  • other protein should be taken to mean any other proteins present in the whey protein source other than GMP, including but not limited to ⁇ -lactalbumin, ⁇ - lactoglobulin, immunoglobulins and serum albumin.
  • the starting material for preferred process of the present invention is a whey protein source.
  • whey protein source any whey protein can be used though the preference is for use of higher protein whey protein product.
  • the present invention is particularly suitable for whey protein isolate derived from rennet casein whey and cheese whey sources.
  • an initial step of dissolving, dispersing, or a combination of both, whey protein source material in a liquid is provided.
  • the liquid is water or primarily water though this should not be seen as a limitation on the present invention in any way for the liquid could conceivably be any solvent which met the requirements of the isolation process.
  • aqueous solution of whey protein is prepared though it is also permissible that some non-dissolved material may be present. It is envisaged that in most cases the undissolved material will merely be separated at a later stage in the procedure.
  • the amount of protein source present in the liquid is in the inclusive range of 9 ⁇ 5 %, optimally between 9 ⁇ 2 %.
  • Protein contents outside of this range are also permissible though in most cases it is considered unlikely that contents above 20%, or below 2% will be considered commercially viable.
  • the inventors have found that outside of these ranges the ability to separate GMP from the whey protein is impaired, or the yields of GMP are too low.
  • the pH of the whey protein should be adjusted to be mildly acidic, to within the pH range of 5.5 through 7.0 inclusive.
  • pH 6.0 was found to give the highest purity of GMP, though this was still very low at 39.6% and as such not commercially viable. There was also no further testing conducted at other pHs surrounding pH 6.0.
  • the inventors have identified the preferred pH of the whey protein to be within a narrower range of 5.8 ⁇ 0.3 pH units, inclusive. Their experiments also showed that GMP yields and purity changed markedly over small pH changes, an observation not shown by Saito et al, 1991 which used large pH steps by comparison, being 1.0 pH units.
  • the whey protein is then heated to denature the majority of protein and/or aggregates in the source with minimal denaturation of the GMP, which remains soluble.
  • Heat denaturation of the whey protein source has previously been used in the art to isolate GMP from whey. While a range of conditions could conceivably be used to isolate GMP, it is essential to identify conditions which will produce high yields of GMP at a high purity without resulting in excessive levels of GMP denaturation.
  • the heat treatment conditions necessary for commercially viable industrial use were selected by the inventors on the basis of three criteria: firstly, the purity of the GMP obtained; secondly, the yield of GMP in the supernatant after separation; and thirdly the ease at which the precipitate could be separated from the soluble GMP phase after heat denaturation. Typically this will involve heating to a temperature exceeding 85°C but typically less than 125°C.
  • the whey protein is heated to within the range of 90°C to 110°C inclusive.
  • the whey protein is heated at 95°C.
  • time and temperature are linked if the desired results are to be attained.
  • a duration of approximately 2-30 minutes has been found by the inventors to produce industrially acceptable levels of GMP purity and yield.
  • the liquid may be heated to a temperature above 110°C but not exceeding 125°C for a period of time within the range of 30 seconds through 5 minutes inclusive.
  • heating of the bulk liquid should be relatively rapid.
  • time typically be commenced when the temperature exceeds 85°C, or for the higher temperature examples above (e.g. 110-120°C), from when the temperature range is entered.
  • the liquid and its contents are cooled to within the range of 50 ⁇ 20°C inclusive.
  • Different cooling methods may be employed, such as by the addition of another cooler liquid, or by heat exchange processes.
  • This cooling step was found to be required to enable the precipitate to be industrially separated from the soluble GMP phase after heat denaturation and to avoid denaturation of GMP that occurs because of extended periods at higher temperatures.
  • Separation may occur by a number of methods known to a skilled addressee.
  • the separation of the soluble portion from the precipitate is by way of filtration or centrifugation.
  • the inventors required a set of conditions that would produce a strong precipitate that was separable from the supernatant using existing dairy clarifiers.
  • the heat denaturation step of the present invention produced such a precipitate.
  • the density difference between the precipitate and the soluble phase is preferably improved by dilution of the liquid and its contents to around 7% total solids. Higher dilutions are possible and result in GMP of similar purities and yields but processing costs increase from the need to remove the additional water.
  • the inventors have also found that dilution of the liquid is required to reduce the sedimentable solids loading to the clarifier. If the dilution step was no undertaken then the high solid levels were found to reduce the efficiency of the clarifier, resulting in precipitate being carried over into the soluble phase and causing a reduction in GMP purity.
  • a method substantially as described above, including a step in which dissolved components are recovered from the soluble portion to yield a GMP-rich product.
  • the recovery of a solid GMP product includes evaporation, and/or spray drying.
  • the GMP-rich dissolved components may be desalted and/or lactose reduced by ultrafiltration before subsequently being dried to yield the GMP-rich product.
  • ultrafiltration is carried out using a membrane of lOkDa or smaller, to prevent loss of GMP through the membranes.
  • Nanofiltration is also suitable when only water and salts are to be removed.
  • These further steps may include the hydrolysis of the protein, preferably by enzyme hydrolysis.
  • non-soluble components are mixed to a slurry of 15% solids or less by weight prior to proteolytic enzyme treatment.
  • the slurry contains 7.5 ⁇ 2.5% inclusive of solids, by weight which has been found by the inventors to be the best conditions for which to undertake this reaction.
  • the slurry may then be subjected to proteolytic enzyme treatment, the conditions of which are sufficient to digest all the protein aggregates to yield soluble peptides.
  • proteolytic enzyme treatment the conditions of which are sufficient to digest all the protein aggregates to yield soluble peptides.
  • Any of a number of commercially available food grade proteolytic enzyme preparations may be used, including for example (but not restricted to): alcalaseTM, trypsin, and protexTM 6L.
  • proteolysis is performed for a period of time within the range of 0.5 through 24 hours, or for as long a period as is desirable. Typically the time range is within one through 18 hours inclusive.
  • the temperature and pH range can be altered in accordance with the appropriate conditions known for the selected enzyme preparation(s).
  • the enzyme is preferably inactivated. This may be simply achieved by heating the reaction mixture to a suitable inactivation temperature for the enzyme being used.
  • the soluble fraction after proteolytic enzyme treatment is dried through such techniques as evaporation and/or spray drying to yield a solid
  • whey protein hydrolysate material prepared according to a method substantially as described above.
  • Figure 1 is a schematic flow chart for one preferred embodiment of the present invention.
  • Figure 2 is schematic flow chart of a variation of the process according to the present invention.
  • the inventors conducted a series of experiments to determine the optimum conditions that allow GMP to be isolated at a high yield and purity without significant GMP denaturation.
  • the heat denaturation step was found to involve heating to a temperature exceeding 85°C but typically less than 125°C.
  • Figures 1 and 2 illustrate in detail processes according to the present invention enabling a casein glycomacropeptide rich product, and low-lactose whey protein hydrolysate product to be obtained.
  • the following description should be read in conjunction with these figures, and in particular with reference to Figure 1.
  • Any dairy whey protein source containing casein glycomacropeptide such as whey protein isolate made by anion exchange or micro filtration or whey protein concentrate, both from rennet casein whey or cheese whey sources.
  • the insoluble precipitate (from step 7) is mixed to a slurry at 10% solids or less. Depending on the centrifugation separation method used in step 7, the addition of water may be required to dilute to 10%.
  • This slurry is subjected to proteolytic enzyme treatment to digest the protein aggregates yielding soluble peptides.
  • proteolytic enzyme treatment can be achieved with the use of commercial enzyme preparations - including for example (but not restricted to): alcalaseTM, trypsin, and protexTM 6L - over an 18 hour period at a temperature and within a pH range appropriate for the enzyme used.
  • the enzyme is inactivated by heating the solution at the inactivation temperature for the enzyme used before evaporating and spray-drying to yield the whey protein hydrolysate.
  • the casein glycomacropeptide product can be desalted and lactose reduced, after centrifugation in step 7, by an ultrafiltration step using membranes of lOkDa or smaller, before spray drying.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Polymers & Plastics (AREA)
  • Food Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Biophysics (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Toxicology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • General Chemical & Material Sciences (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Nutrition Science (AREA)
  • Peptides Or Proteins (AREA)

Abstract

La présente invention se rapporte à une étape d'un procédé de séparation de glycomacropeptides de caséine à partir d'une source de protéines lactosériques. Cette étape consiste en un chauffage de la source de protéines lactosériques sous forme liquide, dans des conditions sélectionnées pour assurer une dénaturation minimale des glycomacropeptides de caséine mais permettre la dénaturation de la majorité des autres protéines et/ou agrégats présents dans la source, lesdites conditions consistant à chauffer la source de protéines lactosériques à une température comprise entre 85° et 125 °C pendant un laps de temps compris, de manière inclusive, entre 2 minutes et 30 minutes.
PCT/NZ2001/000265 2000-12-08 2001-11-30 Isolement de glycomacropeptides de caseine a partir de lactoserum par chauffage et denaturation minimale des glycomacropeptides de caseine WO2002045522A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU2002216479A AU2002216479A1 (en) 2000-12-08 2001-11-30 Isolation method

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NZ50874700 2000-12-08
NZ508747 2000-12-08

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WO2002045522A1 true WO2002045522A1 (fr) 2002-06-13

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Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2015059243A1 (fr) * 2013-10-23 2015-04-30 Arla Foods Amba Compositions de protéines de lactosérum dénaturées riches en protéines contenant du caséinomacropeptide (cmp), produits les contenant et utilisations associées
CN109180806A (zh) * 2018-09-26 2019-01-11 哈尔滨工业大学 一种除去乳清蛋白中酪蛋白糖巨肽的方法
US10251726B2 (en) 2011-11-28 2019-04-09 3Shape A/S Dental preparation guide
CN110381743A (zh) * 2017-01-19 2019-10-25 科·汉森有限公司 酪蛋白糖巨肽(cgmp)寡聚体
US10729150B2 (en) 2013-10-23 2020-08-04 Arla Foods Amba High protein, fruit flavoured beverage; high protein, fruit and vegetable preparation; and related methods and food products
US10834934B2 (en) 2013-10-23 2020-11-17 Arla Foods Amba High protein denatured whey protein composition, related products, method of production and uses thereof
US11825860B1 (en) 2023-01-13 2023-11-28 Leprino Foods Company Denatured milk proteins and methods of making them

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Publication number Priority date Publication date Assignee Title
JPH03294299A (ja) * 1990-04-11 1991-12-25 Snow Brand Milk Prod Co Ltd κ―カゼイングリコマクロペプチドの製造法
US5216129A (en) * 1990-04-27 1993-06-01 Nestec S.A. Production of kappa-caseino-glycomacropeptide
JPH05271295A (ja) * 1992-03-30 1993-10-19 Snow Brand Milk Prod Co Ltd κ−カゼイングリコマクロペプチド含有量の高い組成物の製造方法
WO1994015952A1 (fr) * 1993-01-08 1994-07-21 Novo Nordisk A/S Procede de production de glycomacropeptide de kappa-caseine et utilisation d'un glycomacropeptide de kappa-caseine
WO1999029183A1 (fr) * 1997-12-11 1999-06-17 M D Foods A.M.B.A. Procede de preparation d'un glycomacropeptide kappa-caseinique ou d'un derive
WO2001011990A1 (fr) * 1999-04-29 2001-02-22 Societe Des Produits Nestle S.A. Composition a faible teneur en threonine destinee a une formule pour enfant

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH03294299A (ja) * 1990-04-11 1991-12-25 Snow Brand Milk Prod Co Ltd κ―カゼイングリコマクロペプチドの製造法
US5216129A (en) * 1990-04-27 1993-06-01 Nestec S.A. Production of kappa-caseino-glycomacropeptide
JPH05271295A (ja) * 1992-03-30 1993-10-19 Snow Brand Milk Prod Co Ltd κ−カゼイングリコマクロペプチド含有量の高い組成物の製造方法
WO1994015952A1 (fr) * 1993-01-08 1994-07-21 Novo Nordisk A/S Procede de production de glycomacropeptide de kappa-caseine et utilisation d'un glycomacropeptide de kappa-caseine
WO1999029183A1 (fr) * 1997-12-11 1999-06-17 M D Foods A.M.B.A. Procede de preparation d'un glycomacropeptide kappa-caseinique ou d'un derive
WO2001011990A1 (fr) * 1999-04-29 2001-02-22 Societe Des Produits Nestle S.A. Composition a faible teneur en threonine destinee a une formule pour enfant

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
SAITO T. ET AL.: "A new isolation method of caseinoglycopeptide from sweet cheese whey", JOURNAL OF DAIRY SCIENCE, vol. 74, 1991, pages 2831 - 2837 *

Cited By (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US11478330B2 (en) 2011-11-28 2022-10-25 3Shape A/S Dental preparation guide
US10251726B2 (en) 2011-11-28 2019-04-09 3Shape A/S Dental preparation guide
US11903779B2 (en) 2011-11-28 2024-02-20 3Shape A/S Dental preparation guide
US11653998B2 (en) 2011-11-28 2023-05-23 3Shape A/S Dental preparation guide
US10918458B2 (en) 2011-11-28 2021-02-16 3Shape A/S Dental preparation guide
EA035744B1 (ru) * 2013-10-23 2020-08-05 Арла Фудс Амба Содержащие cmp высокобелковые композиции денатурированного сывороточного белка, содержащие их продукты и их применения
KR20160075657A (ko) * 2013-10-23 2016-06-29 아를라 푸즈 에이엠비에이 Ｃｍｐ-함유, 고단백질 변성 유장 단백질 조성물, 그들을 함유하는 제품 및 그의 용도
US10709146B2 (en) 2013-10-23 2020-07-14 Arla Foods Amba CMP-containing, high protein denatured whey protein compositions, products containing them, and uses thereof
US10834934B2 (en) 2013-10-23 2020-11-17 Arla Foods Amba High protein denatured whey protein composition, related products, method of production and uses thereof
US10729150B2 (en) 2013-10-23 2020-08-04 Arla Foods Amba High protein, fruit flavoured beverage; high protein, fruit and vegetable preparation; and related methods and food products
KR102362483B1 (ko) 2013-10-23 2022-02-14 아를라 푸즈 에이엠비에이 Ｃｍｐ-함유, 고단백질 변성 유장 단백질 조성물, 그들을 함유하는 제품 및 그의 용도
WO2015059243A1 (fr) * 2013-10-23 2015-04-30 Arla Foods Amba Compositions de protéines de lactosérum dénaturées riches en protéines contenant du caséinomacropeptide (cmp), produits les contenant et utilisations associées
EP3366145A1 (fr) * 2013-10-23 2018-08-29 Arla Foods amba Compositions de protéines de lactosérum dénaturées riches en protéines contenant du caséinomacropeptide (cmp), produits les contenant et utilisations associées
CN110381743A (zh) * 2017-01-19 2019-10-25 科·汉森有限公司 酪蛋白糖巨肽(cgmp)寡聚体
CN109180806A (zh) * 2018-09-26 2019-01-11 哈尔滨工业大学 一种除去乳清蛋白中酪蛋白糖巨肽的方法
US11825860B1 (en) 2023-01-13 2023-11-28 Leprino Foods Company Denatured milk proteins and methods of making them

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