WO1992011770A1 - Procede de separation de proteines de lactoserum et produits obtenus - Google Patents

Procede de separation de proteines de lactoserum et produits obtenus Download PDF

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Publication number
WO1992011770A1
WO1992011770A1 PCT/FR1992/000005 FR9200005W WO9211770A1 WO 1992011770 A1 WO1992011770 A1 WO 1992011770A1 FR 9200005 W FR9200005 W FR 9200005W WO 9211770 A1 WO9211770 A1 WO 9211770A1
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WIPO (PCT)
Prior art keywords
whey
proteins
precipitation
lactoglobulin
lactalbumin
Prior art date
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PCT/FR1992/000005
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English (en)
French (fr)
Inventor
Jean-Jacques Maugas
Christine Le Magnen
Original Assignee
Societe Eurial
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 Societe Eurial filed Critical Societe Eurial
Priority to PL29586392A priority Critical patent/PL295863A1/xx
Publication of WO1992011770A1 publication Critical patent/WO1992011770A1/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
    • 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
    • C07K14/4717—Plasma globulins, lactoglobulin
    • 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
    • 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
    • C07K14/76—Albumins
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/04—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from milk
    • 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
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the subject of the invention is a process for the separation of whey proteins and the products obtained.
  • whey represents the soluble phase of milk after elimination of the casein fraction.
  • cheese manufacturing, casein manufacturing processes (acids or rennets), or even the use of microfiltration membranes we will mention cheese manufacturing, casein manufacturing processes (acids or rennets), or even the use of microfiltration membranes.
  • Whey proteins have the advantage of being remarkably balanced in amino acids. Among these proteins, a main distinction is made, in decreasing concentration, ⁇ -lactoglobulin, ⁇ -lactalbumin, bovine serum albumin, immunoglobulins, peptone proteases, and lactoferrin.
  • the protein fraction represents 5 to 10% of the total dry extract. We therefore measure the value of separating it from other less valuable components such as lactose, residual lipids, mineral salts and isolating each of the protein constituents, taking into account their own value.
  • Adsorption on ion exchangers precipitation with various agents, in particular polyelectrolytes, that is to say products comprising several charges.
  • the main precipitating agents used are carboxymethylcellulose, polyacrylic acid, ferric chloride, polyethylene glycol, chitosan, bentonite, lignosulfate, sodium laurysulfate.
  • the precipitated fraction is generally not pure and contains part of the residual whey lipids which also precipitate by these methods.
  • the inventors have found that it is possible to remedy these drawbacks and to obtain proteins of high purity by treating the whey so as to give it determined characteristics and by specifically controlling the precipitation conditions for each protein to be separated.
  • the invention therefore aims to provide a process for recovering from whey, proteins of high biological value, in a form of high purity.
  • the process according to the invention for separating whey proteins is characterized in that a whey concentrated in proteins, and where appropriate delipidated, is used as raw material, and that the ⁇ -lactoglobulin is isolated by precipitation and then, if it is desired, the other proteins of interest, by sequential addition of precipitating agents in an acid medium to the concentrated whey, then to the soluble phases successively formed as ⁇ o-products of the protein precipitates.
  • whey is meant both a sweet whey from cheese or rennet casein and an acid whey also from cheese or acid casein. It can also be the soluble milk phase (microfiltrate) obtained by microfiltration of whole or skimmed milk using a membrane. Whey is obtained from milk, colostrum, or is: "recons i ued from powder.
  • concentrated whey provides a raw material with a higher protein / dry extract ratio than in the whey, with a mineral matter / protein ratio favoring the envisaged separations.
  • the whey is advantageously subjected to a treatment which makes it possible to have a soluble phase free of at least most, if not all, of the non-protein constituents.
  • At least one ultrafiltration operation is used using membranes which specifically retain the proteins present and allow the lactose, mineral salts and small nitrogenous molecules (non-protein nitrogenous fraction) to pass through.
  • the operation is preferably carried out at a temperature above ambient, in particular from 30 ° to 60 ° C. approximately.
  • the concentrate is obtained by adding concentrated whey proteins to crude whey, more particularly in powder form.
  • the retentate thus obtained has a concentration of approximately 12 to 90 g / kg, more particularly approximately 20 to 40 g / kg of proteins / kg and a nitrogenous matter / dry extract ratio of the order of 20 to 70%, more especially of the order of 30 to 40%.
  • thermocalcic aggregation or not of the lipids via calcium ions The elimination of the lipid fraction of the whey is made possible by thermocalcic aggregation or not of the lipids via calcium ions and elimination of the aggregates obtained by microfil ration or centrifugal separation according to the methods described by FAUQUANT et al. in Milk 65 (1) 1-20, 1985 and Maubois et al. in Bulletin of the IDF 212, chapter 24, 154-159, 1987.
  • this step is carried out on a retentate obtained by ultrafiltration of whey as described above, with or without the addition of calcium.
  • Delipidation advantageously makes it possible to increase the purity of the purified proteins, which gives them better functional properties.
  • whey often contains "fines" of casein which are advantageously removed during the delipidation step by the physical techniques employed.
  • precipitating agents are added sequentially to the acidic phases.
  • these are polyéle ⁇ trolytes.
  • the polyelectrolytes used are more especially chosen from the phosphate salts or derivatives of phosphoric acids.
  • polymetaphosphates such as Graham salts, sodium hexametaphosphate, potassium hexametaphosphate, or alternatively pyrophosphates, polyphosphates, salts derived from phosphoric acid, or mixtures of two or more of these compounds.
  • the concentration of polyelectrolytes in the first separation step depends on the concentration of ⁇ la ⁇ toglobulin in the starting whey. It is, for example, from 4 to 20% by weight approximately relative to the concentration of the protein during the use of phosphate salts, in particular of the order of 5 to 16% by weight.
  • the addition of the salts is advantageously carried out at a temperature of about 0 to 35 ° C, preferably close to ambient.
  • acidification is carried out to adjust the pH to a value leading to the precipitation of ⁇ -lactoglobulin.
  • the pH is advantageously adjusted in the range of 4.9 to 4.00 depending on the retentates used.
  • the acidification is carried out by adding an organic or mineral acid, with stirring.
  • organic or mineral acid By way of example, mention will be made of hydrochloric, sulfuric and phosphoric acid for mineral acids and lactic acid for organic acids.
  • a decanter a centrifuge, a clarifier, a microfiltration or ultrafiltration installation equipped with membranes having a cutoff threshold such as the soluble phase and the constituents which compose it pass through the membrane and the precipitated phase is retained, these devices operating continuously or not.
  • a decanter a centrifuge, a clarifier, a microfiltration or ultrafiltration installation equipped with membranes having a cutoff threshold such as the soluble phase and the constituents which compose it pass through the membrane and the precipitated phase is retained, these devices operating continuously or not.
  • One can also operate by decantation in a tank or a tank, under the effect of atmospheric pressure.
  • the precipitated phase represents from 5 to 20% by weight approximately of the raw material used, more particularly from 8 to 12% when using a decanter or a clarifier, techniques which will be favorite.
  • the precipitated phase thus obtained has a protein / dry extract weight ratio of approximately 85 to 95%.
  • ⁇ -lactoglobulin represents approximately 85 to 90% by weight of the proteins of this precipitated phase when the raw material has not been defatted.
  • ⁇ -lactoglobulin represents up to approximately 90 to 95% of the proteins of the precipitated phase, which shows the high specificity of the separation process of the invention with regard to the isolation of ⁇ - lactoglobulin.
  • the precipitate obtained can be redissolved by adding an alkali in order to obtain a pH value of the order of 5.5 to 8.0.
  • alkaline product mention will be made of soda, potash or even ammonia.
  • This solution is dried for example by atomization or lyophilized. As a variant, it is concentrated before drying by ultrafiltration and, where appropriate, diafiltration or reverse osmosis.
  • the ⁇ -lactoglobulin solution can also be diafiltered to increase the protein / solids ratio.
  • the alkaline solution of ⁇ -lactoglobulin is subjected to an anion exchange chromatography, carried out according to conventional techniques.
  • Suitable anion exchange resins include those sold under the brands Dowex R 1 x 1, Dowex R 1 x 2, Dowex R 1 x 4, Amberlite R, IRA R 401, and preferably Duolite A 102 D.
  • the procedure is as described above for the first separation of proteins with the soluble phases which separate from the precipitates successively formed during the addition of precipitating agents in acid medium.
  • the co-product or soluble phase resulting from the first precipitation contains at least the major part of the other proteins of the starting concentrated whey. It is in the form of a translucent liquid.
  • the concentration of ⁇ -lactalbumin in this solution depends on the initial concentration of the retentate used and conditions the amount of additional polyelectrolytes necessary to cause protein aggregation in an acid medium.
  • this amount varies from about 2 to 35% by weight of the weight concentration of ⁇ -lactalbumin in the case where the polyelectrolyte used is a phosphate salt such as sodium hexametaphosphate.
  • the addition of the salts is advantageously carried out at a temperature of about 0 to 35 ° C.
  • the pH is adjusted after addition of the salts to a value advantageously of the order of 2.4 to 4.00.
  • the acidification is carried out by adding an organic or mineral acid with stirring.
  • the separation of the precipitate is carried out using the same methods as those described above for the first separation. After separation, and according to the technique used to effect this separation, the precipitated phase represents from 2 to 20% approximately of the weight of the soluble phase used.
  • the precipitated phase thus obtained has a protein / dry extract weight ratio of the order of 85 to 95%.
  • the ⁇ -lactalbumin represents approximately 75 to 85% by weight of the proteins of this precipitate. We therefore measure the interest of the process of the invention which makes it possible to obtain this protein in large quantities.
  • the method of the invention can also be used to obtain glycomacropeptide.
  • GMP glycomacropeptide
  • this peptide remains in the non-precipitated soluble phase.
  • the glycomacropeptide is still soluble and represents the majority of the nitrogen components of the second precipitation supernatant.
  • the supernatant containing the glycomacropeptide in solution results alternatively from the joint precipitation of ⁇ -lactoglobulin and ⁇ -lactalbumin by using an amount of precipitating agent suitable for this purpose and by adjusting the pH to a value of the order from 2.5 to 4.00.
  • the molecular weight constituents of about 3,000 to 10,000 daltons are removed from the soluble phase.
  • the ultrafiltration is carried out using membranes having a cutoff threshold of approximately 3,000 to 10,000 daltons.
  • the membranes used can be organic membranes, called second generation, or mineral membranes, called third generation.
  • the concentrate thus obtained has a weight nitrogen / dry extract weight ratio which varies from 75 to 90% approximately and the glycomacropeptide represents from 80 to 95% by weight approximately of this nitrogen material.
  • proteins present in the soluble co-product phases of precipitation can be isolated, if desired, by operating as indicated above with adjustment of the concentration of pre-digesting agent and of the pH.
  • the invention therefore provides the means of obtaining high-value proteins on an industrial scale. biological and high purity which is of major interest for the biological applications of these products.
  • the invention relates more specifically to the ⁇ -lactalbumin and the glycomacropeptide of high purity thus obtained.
  • soluble phases co-products of the precipitates formed during the implementation of the process of the invention.
  • These soluble phases are formed from concentrated whey free of at least the major part of the non-protein constituents from which a given protein has been eliminated at each separation step.
  • This is in particular the soluble phase as obtained from the first separation, essentially containing as a protein constituent of ⁇ -lactalbumin and according to the nature of the starting whey of glycomacropeptide.
  • UF 1 retentate The retentate thus obtained, called UF 1 retentate, is then defatted by microfiltration on mineral membranes having a cutoff threshold of 0.14 ⁇ .
  • the defatted microfiltrate is concentrated 2 times by ultrafiltration using the same material as that used for the initial concentration of the whey.
  • the concentrate obtained by this second ultrafiltration constitutes the raw material for the separation of proteins.
  • Table 1 summarizes the evolution of nitrogen concentrations and dry extracts of the various products.
  • the precipitate is diluted with a volume of water and the pH is adjusted to 6.5 by adding sodium hydroxide with stirring.
  • the precipitate resolubilizes at this pH value and has the appearance of a translucent orange solution. This solution is frozen and then lyophilized.
  • polyelectrolytes 27% are added relative to the weight of ⁇ -lactalbumin present in the solution.
  • the polyelectrolyte chosen is a polyphosphate salt.
  • the pH of the solution is adjusted, after dissolution of the salts, to 3.5 by addition of hydrochloric acid.
  • the precipitate is separated from the soluble phase by centrifugation at 4,000 g for 5 minutes. The balance by weight shows that the precipitated fraction represents 8% and the supernatant phase 92%.
  • the evolution of the protein distribution is indicated in Table 3.
  • the precipitate 2 is diluted with an equivalent volume of water and the pH is adjusted to 6.5 by addition of sodium hydroxide. The resolubilization is complete and the solution thus obtained is diafiltered on an ultrafiltration installation equipped with organic membranes having a cutoff threshold of 10,000 daltons.
  • Diafiltration uses 4 volumes of water per volume of protein solution. The diafiltered solution is then frozen and lyophilized.
  • the soluble phase 2 is concentrated by ultrafiltration on an installation equipped with organic membranes having a cutoff threshold of 3000 daltons.
  • the concentration factor is 5.
  • the retentate thus obtained is diafiltered with 6 volumes of water.
  • 100 liters of skimmed milk are microfiltered on an installation equipped with microfiltration membranes having a cutoff threshold of 0.14 ⁇ m.
  • the temperature is 50 ° C and the pH 6.6.
  • the volume concentration factor is 2.
  • the 50 liters of microfiltrate recovered are then concentrated on an ultrafiltration installation equipped with organic membranes.
  • the concentration factor applied is then 5.
  • the polyelectrolyte agent chosen for the separation is a mixture of phosphate salts containing 85% sodium hexametaphosphate and 15% sodium tripolyphosphcite.
  • the amount of added salts represents 9.5% of the ⁇ -lactoglobulin contained in the raw material of departure.
  • the pH is adjusted to 4.37 by addition of hydrochloric acid.
  • the precipitate is separated from the soluble phase by centrifugation at 2500 g for 4 minutes.
  • the weight of precipitate represents 11% of the weight of retentate used, the supernatant 89%.
  • the precipitate is diluted with 3 volumes of water and redissolved by adding sodium hydroxide.
  • the solution is then at pH 7.0.
  • This solution is concentrated 5 times by ultrafiltration using organic membranes.
  • soluble phase 1 4 liters of soluble phase 1 are added with phosphate salts (same mixture of the two salts as above).
  • the amount of polyelectrolyte agent represents 22% of the amount of ⁇ -lactalbumin present in the soluble phase.
  • the pH is adjusted to 3.15 by addition of hydrochloric acid with stirring.
  • the precipitate of ⁇ -lactalbumin thus obtained is separated by centrifugation at 5000 g for 10 minutes.
  • the protein composition of the precipitate is 65.9 g / kg of ⁇ -lactalbumin and 6.33 g / kg of ⁇ -lactoglobulin, ie an ⁇ -lacta / ⁇ -lacta + ⁇ -lacto ratio of 91.2%.
  • the precipitate 2 is taken up in 2 volumes of water and the pH is adjusted to 4.8 by addition of sodium hydroxide.
  • This solution of ⁇ -lactalbumin is chromatographed on an anion exchanger in 0H form
  • the solution recovered after ion exchange has a pH value of 8.5. It is concentrated by ultrafiltration on a device equipped with organic membranes having a cutoff threshold of 10,000 daltons. The volume concentration factor is 2. The retentate is then diafiltered by a volume of water. The final solution has a total ⁇ -lactalbumin / nitrogenous matter ratio of 90.5%.
  • a tank allowing the recovery of the precipitate by an alkali, with a stirring system, equipped with a metering pump delivering the alkali (subject to pH measurement) and advantageously comprising an element for controlling and regulating pH.
  • This device can be doubled for a second precipitation or can operate in batch with storage of the supernatant phase separated from the precipitate and resumption of this phase in the first tank at the end of the first precipitation cycle.

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  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Molecular Biology (AREA)
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  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
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  • Gastroenterology & Hepatology (AREA)
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PCT/FR1992/000005 1991-01-03 1992-01-03 Procede de separation de proteines de lactoserum et produits obtenus WO1992011770A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
PL29586392A PL295863A1 (en) 1991-01-03 1992-01-03 Method of isolating from whey

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FR91/00035 1991-01-03
FR9100035A FR2671351A1 (fr) 1991-01-03 1991-01-03 Procede de separation de proteines de lactoserum et produits obtenus.

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WO1992011770A1 true WO1992011770A1 (fr) 1992-07-23

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AU (1) AU1178692A (US06432973-20020813-C00010.png)
FR (1) FR2671351A1 (US06432973-20020813-C00010.png)
IE (1) IE920012A1 (US06432973-20020813-C00010.png)
PL (1) PL295863A1 (US06432973-20020813-C00010.png)
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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2019076851A1 (fr) * 2017-10-20 2019-04-25 Groupe Lactalis Concentrat ou isolat de proteines solubles de lait stable au cours des traitements thermiques, et procede d'obtention.
CN112770637A (zh) * 2018-06-27 2021-05-07 阿尔拉食品公司 制备富含α-乳白蛋白的组合物、相关产品的新方法及在例如婴儿配方食品中的用途

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CA2431842C (en) * 2000-12-06 2011-08-09 Campina Melkunie B.V. Method for preparing tryptophan rich peptides

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2264818A1 (US06432973-20020813-C00010.png) * 1974-03-20 1975-10-17 Stauffer Chemical Co

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2264818A1 (US06432973-20020813-C00010.png) * 1974-03-20 1975-10-17 Stauffer Chemical Co

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, vol. 105, no. 1, 7 Juillet 1986, Columbus, Ohio, US; abstract no. 5359V, A W SLACK ET AL.: 'production of enriched beta-lactoglobulin and alpha-lactalbumin whey protein fractions' page 516 ; *
CHEMICAL ABSTRACTS, vol. 97, no. 21, 22 Novembre 1982, Columbus, Ohio, US; abstract no. 180496A, C H AMUNDSON ET AL.: 'production of enriched protein fractions of beta-lactoglobulin and alpha-lactalbumin from cheese whey' page 654 ; *
JOURNAL OF FOOD SCIENCE. vol. 50, no. 6, 1 Novembre 1985, CHICAGO US pages 1531 - 1536; T KANEKO ET AL: 'selective concentration of bovine immunoglobulin and alpha-lactalbumin from acid whey using iron chloride(III)' cité dans la demande *

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2019076851A1 (fr) * 2017-10-20 2019-04-25 Groupe Lactalis Concentrat ou isolat de proteines solubles de lait stable au cours des traitements thermiques, et procede d'obtention.
FR3072542A1 (fr) * 2017-10-20 2019-04-26 Groupe Lactalis Concentrat ou isolat de proteines solubles de lait stable au cours des traitements thermiques, et procede d'obtention.
CN112770637A (zh) * 2018-06-27 2021-05-07 阿尔拉食品公司 制备富含α-乳白蛋白的组合物、相关产品的新方法及在例如婴儿配方食品中的用途

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IE920012A1 (en) 1992-07-15
FR2671351A1 (fr) 1992-07-10
PL295863A1 (en) 1994-02-21
FR2671351B1 (US06432973-20020813-C00010.png) 1995-03-24
AU1178692A (en) 1992-08-17

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