WO1995019714A1 - Process for fractionating whey proteins and the components so obtained - Google Patents
Process for fractionating whey proteins and the components so obtained Download PDFInfo
- Publication number
- WO1995019714A1 WO1995019714A1 PCT/FI1995/000027 FI9500027W WO9519714A1 WO 1995019714 A1 WO1995019714 A1 WO 1995019714A1 FI 9500027 W FI9500027 W FI 9500027W WO 9519714 A1 WO9519714 A1 WO 9519714A1
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- WIPO (PCT)
- Prior art keywords
- whey
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- component
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- solution
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/14—Milk preparations; Milk powder or milk powder preparations in which the chemical composition of the milk is modified by non-chemical treatment
- A23C9/146—Milk preparations; Milk powder or milk powder preparations in which the chemical composition of the milk is modified by non-chemical treatment by ion-exchange
- A23C9/1465—Chromatographic separation of protein or lactose fraction; Adsorption of protein or lactose fraction followed by elution
-
- 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
Definitions
- the invention relates to a process for fractionating whey proteins. More specifically, the invention relates to a process for fractionating whey or whey protein solution chromatographically select ⁇ ively into an alpha-lactalbumin component and a beta- lactoglobulin component, and to an alpha-lactalbumin component and beta-lactoglobulin component so obtained.
- the obtained alpha-lactalbumin component is as such suitable for use in infant food formulas
- the obtained beta-lactoglobulin component in turn is as such suitable for use as a protein component in clinical nutritive preparations and various products of the food industry.
- Milk whey proteins are used inter alia in infant food formulas on account of their high digestibility and excellent nutritional value.
- the pro ⁇ tein of infant food formulas is composed of milk casein and whey protein in a ratio of 40:60 (casein: whey protein) , which corresponds to the ratio between casein and whey protein in human milk.
- the protein composition of infant food formulas does not fully correspond to that of human milk, as the whey protein of cow's milk differs in composition from the whey protein of human milk; human milk contains no beta-lactoglobulin ( ⁇ -LG), which is the main component of the whey protein of cow's milk.
- ⁇ -LG beta-lactoglobulin
- the whey protein of cow's milk alpha-lactalbumin ( ⁇ - LA)
- ⁇ - LA alpha-lactalbumin
- the protein of human milk is mainly composed of - LA (approx. 40% by weight)
- ⁇ -LG As certain functional properties of ⁇ -LG (such as solubility within a wide pH range and good gelific- ation ability) are clearly better than those of whey protein concentrate (WPC), ⁇ -LG is regarded as well suited for use in the food industry. At present, the food industry uses WPC but is waiting for the entry into market of an economically feasible beta-lacto ⁇ globulin [D.M. Mulvihill, Food Research Quarterly 51 (1991) 65-73]. WPC is used e.g. in clinical nutritive preparations. In yoghurts, fresh cheeses and curd, it is used to replace casein. In curd, as much as 20% by weight of the casein can be replaced with whey pro ⁇ tein.
- WPC fatless WPC
- flavoured milk drinks such as cocoa
- WPC has also been used in the production of ice-cream, ice-lollies, meringue (only fatless WPC) and chocolate coatings [D. M. Mulvihill, Food Research Quarterly 51 (1991), 65-73].
- Spherosil QMA resin is composed of silica particles (diameter between 100 and 300 ⁇ m) coated with styrene vinyl triethoxysilane co- polymer to which quaternary ammonium groups are attached. This resin has a mean pore size of 1,250 A, a pore volume of 1 cm 3 /g and a specific surface area of 25 m 2 /g.
- Example 8 the Thibault process allows native whey (ash content less than 1% by weight) to be treated only within a pH range be ⁇ tween 4 and 6. Whey with a high salt content (ash content between 1 and 3% by weight) can be treated within a pH range between 6 and 8.
- the object of this invention is to provide an industrially applicable process which avoids the above-mentioned drawbacks and which allows whey or whey protein solution to be fractionated selectively into an alpha-lactalbumin component and a beta-lacto ⁇ globulin component.
- the invention relates to a process for frac ⁇ tionating whey or whey protein solution chromato- graphically selectively into an alpha-lactalbumin component and a beta-lactoglobulin component.
- the process is characterized by a) clarifying a batch of whey or whey protein solution and, if required, removing glycomacropeptides from it; b) passing whey or whey protein solution treated at stage a) through a chromatography column packed with a strong polystyrene-based anion exchange resin, which resin has a great pore size ranging between 1,000 and 2,000 A and a pore volume of at least 0.9 cm 3 /g and in which quaternary alkyl amine or alkyl alkanoamine groups, preferably alkyl alkanoamine groups, are attached to a styrene-divinyl-benzene- polymer matrix, and which has a particle diameter between 300 and 600 ⁇ m, and recovering the fraction leaving the
- the process according to the invention is suitable for fractionating proteins from different types of wheys and whey protein solutions, such as cheese and casein whey, demineralized whey and whey protein concentrate. It is particularly well suited for fractionating casein whey into an alpha-lact- albumin component and a beta-lactoglobulin component.
- whey or whey protein solution can be fractionated more effect ⁇ ively than previously by the strong anion exchange resins Diaion HPA 25 and HPA 75 (Resindion, Mitsubishi Kasei Corp., Japan), which are much cheaper than the Spherosil QMA resins.
- Quaternary alkyl amine (HPA 25) or alkyl alkanoamine (HPA 75) groups are attached to the styrene-divinyl-benzene-poly er matrix of these HPA resins. Due to their great pore size (1,000 to 2,000 A), pore volume (0.9 cm 3 /g) and specific surface area (23 to 25 m 2 /g), these HPA resins are suitable for separating large molecules.
- HPA resins The price of the HPA resins is only about 1/100 of that of the Spherosil QMA resins.
- HPA resins are well suited for industrial applications on account of their appropriate particle size (diameter 300 too 600 ⁇ m) and mechanical strength.
- a further advantage of the HPA resins is that protein attached to them can be eluted by a 2 to 5 wt.% NaCl solution, whereas less safe hydrochloric acid has to be used to elute protein attached to Spherosil QMA resin in the process described by P.J. Skudder in J. Dairy Res . , 52 (1985), 167-181.
- the NaCl treatment is also to be preferred over HC1 from the viewpoint of preserving the nativity of the protein.
- the process according to the invention allows most of ⁇ -LG to be separated from native whey (ash content less than 1% by weight) into a fraction substantially free of other whey proteins within a pH range between 6 and 7 without pH adjustment, whereas native whey can be treated in the process described in US Patent 5,077,067 only within a pH range between 4 and 6.
- the attached drawings give chromatograms obtained by Fast Protein Liquid Chromatography, FPLC, for the alpha-lactalbumin and beta-lactoglobulin fractions of whey.
- Figure 1 shows FPLC chromatograms obtained for the alpha-lactalbumin and beta-lactoglobulin fractions of casein whey with HPA 75 resin according to the in ⁇ vention;
- Figure 2 shows FPLC chromatograms obtained for the alpha-lactalbumin and beta-lactoglobulin fractions of casein whey with Spherosil QMA LS resin.
- whey or whey protein solu ⁇ tion is clarified by precipitating residual casein, phospholipoprotein and calcium phosphate by an in ⁇ crease in pH, an addition of CaCl 2 '2H 2 0 and a light heat treatment, and by removing the precipitate by decantation, centrifugation or microfiltration.
- the clarification method does not significantly affect the protein composition of wheys.
- whey or whey protein solu ⁇ tion treated at process stage a) is passed through a chromatography column packed with a strong poly ⁇ styrene-based anion exchange resin, which resin has a great pore size between 1,000 and 2,000 A and a pore volume of at least 0.9 cm 3 /g and in which quaternary alkyl amine or alkyl alkanoamine groups, preferably alkyl alkanoamine groups, are attached to the styrene- divinyl-benzene-polymer matrix, and which has a par ⁇ ticle diameter between 300 and 600 ⁇ m, and the fraction leaving the column is recovered.
- a strong poly ⁇ styrene-based anion exchange resin which resin has a great pore size between 1,000 and 2,000 A and a pore volume of at least 0.9 cm 3 /g and in which quaternary alkyl amine or alkyl alkanoamine groups, preferably alkyl alkanoamine groups, are attached to the s
- whey or whey protein solution in a corresponding amount with respect to the protein, treated at process stage a), is passed at process stage b) at a pH ranging between 6.0 and 7.0 at a flow rate of 3 to 5 column volumes per hour through a chromatography column packed with a strong polystyrene-based anion exchange resin so that 6 to 7 cm 3 of whey or whey protein solution in a corresponding amount with respect to the protein are passed through the column per 1 cm 3 of resin.
- the anion exchange resin column treated at stage b) is washed with deionized water, the wash water is combined with the fraction recovered at process stage b) and the obtained solu- tion is recovered as an alpha-lactalbumin component.
- the recovered alpha-lactalbumin component can be used as such as an ⁇ -LA component particularly in infant food formulas or it can be concentrated and, if desired, dried in a manner known per se before use as an ⁇ -LA component.
- ⁇ -LG bound to the resin column can be released from the washed anion exchange resin column by eluting with a weak aqueous NaCl solu ⁇ tion, preferably an aqueous 2 to 5 wt.% NaCl solution, and the eluate is recovered as a beta-lactoglobulin component. After having been rinsed with water, the resin is ready for re-use.
- a weak aqueous NaCl solu ⁇ tion preferably an aqueous 2 to 5 wt.% NaCl solution
- the recovered beta-lactoglobulin component can be used as such as a ⁇ -LG component e.g. in clinical nutritive preparations or various products of the food industry. It can also be concentrated and, if desired, dried in a manner known per se before use as a ⁇ -LG component.
- Cheese whey usually contains glycomacropeptide (GMP) formed from milk casein in the production of cheese as a result of the action of a rennet enzyme.
- GMP glycomacropeptide
- GMP deteriorates protein fraction- ation with ion exchange resins [P.J. Skudder, J. Dairy Res . , 52 (1985) 167 - 181] and that it may even cause blocking of Spherosil QMA resin.
- GB Patent Appli ⁇ cation 2,188,526, J. Burton and P.J. Skudder describe a process utilizing Spherosil QMA for removing GMP.
- GMP can be removed from whey or whey protein solution qualit ⁇ atively, as it can be made to attach to the strong anion exchange resin Diaion HPA 25 or HPA 75 at pH 5.0.
- Glycomacropeptides possibly present in whey or whey protein solution at stage a) of the process according to the invention are thus removed by passing clarified whey or whey protein solution at pH 5.0 at a flow rate of 3 to 7 column volumes per hour through a chromatography column packed with strong polystyrene- based anion exchange resin, which resin has a great pore size between 1,000 and 2,000 A and a pore volume of at least 0.9 cm 3 /g and in which quaternary alkyl amine or alkyl alkanoamine groups, preferably alkyl alkanoamine groups, are attached to the styrene- divinyl-benzene-polymer matrix, and which has a par ⁇ ticle diameter between 300 and 600 ⁇ m, so that 7 to 10 cm 3 of whey or whey protein solution in a correspond ⁇ ing amount with respect to the protein are passed through the column per 1 cm 3 of resin, and the fraction leaving the column is passed to stage b).
- Fractionation of whey proteins from cheese whey or cheese whey protein solution purified from GMP is significantly more efficient than from unpurified cheese whey or cheese whey protein solution, and no problems are caused by blocked columns.
- GMP can be removed considerably more economically than in the above-mentioned known process, as the expensive Spherosil QMA resin can now be replaced with the Diaion HPA 25 or HPA 75 resins, which are markedly cheaper.
- HC1 can be replaced with a NaCl solution in eluting Diaion HPA 25 or HPA 75 resins.
- the invention also relates to an alpha-lact ⁇ albumin component which is useful as an ⁇ -LA component particularly in infant food formulas and which is produced by the process according to the invention.
- the invention relates to a beta- lactoglobulin component which is useful as a ⁇ -LG protein component in the food industry in the produc ⁇ tion of e.g. clinical nutritive preparations and dif ⁇ ferent kinds of food products, such as various drinks, sausages and ice-creams, and which is produced by the process according to the invention.
- a beta- lactoglobulin component which is useful as a ⁇ -LG protein component in the food industry in the produc ⁇ tion of e.g. clinical nutritive preparations and dif ⁇ ferent kinds of food products, such as various drinks, sausages and ice-creams, and which is produced by the process according to the invention.
- Example 1
- casein whey (2,000 cm 3 ) was adjusted between 7.5 and 8.5, and the whey was warmed for 30 min at 50°C, after which it was allowed to stand for 16 h at 5°C. Clear whey was separated from the pre ⁇ cipitated calcium phosphate, fat and lipoproteins through decantation. Clarified whey was additionally filtered through Whatman GF/A filter paper and stored at 5°C. 30 cm 3 of regenerated, strong anion exchange resin Diaion HPA 25 were packed into a chromatography column. 200 cm 3 of casein whey clarified as described above were passed through the resin column at a rate of 100 cm 3 /h at pH 6.5.
- Example 1 This example is identical with Example 1 except that the material precipitated in the clarification of whey was separated from whey by centrifugation (4,200 g, 20 min), and the resin was Diaion HPA 75.
- Table 1 shows data on the composition of the ⁇ and ⁇ frac ⁇ tions.
- B bovine serum albumin
- C ⁇ -LG
- D ⁇ -LA
- E orotic acid.
- Example 3 30 cm 3 of regenerated, strong anion exchange resin Spherosil QMA LS were packed into a chromato ⁇ graphy column. 200 cm 3 of casein whey clarified as described in Example 2 were passed through the resin column at a rate of 100 cm 3 /h at pH 6.5. The column was washed with 60 cm 3 of deionized water (100 cm 3 /h) until the absorbance of the solution at the wave length of 280 nm was 0. Whey leaving the column and the wash water were combined (alpha fraction).
- compositions of protein fractions produced as described in Examples 1 to 3 are described in Examples 1 to 3
- the alpha fraction obtained by Diaion HPA 75 was thus of higher quality and had a higher yield than that obtained by Spherosil QMA LS.
- Example 4 8.8 g of CaCl 2 *2H 2 0 were added to cheese whey
- Whey (300 cm 3 ) clarified as described above was passed through a Diaion HPA 75 resin column (30 cm 3 ) at 100 cm 3 /h at pH 5.0. On leaving the column, the whey contained less than 20% of the original GMP. The ⁇ -LA concentration was unaffected by the treatment; less than 9% of the beta-lactoglobulin contained in the feed remained in the resin. GMP attached to the resin was eluted with a 4-wt.% NaCl solution, and salts were washed off the resin by deionized water. The resin was ready for re-use.
- Example 5 Example 5
- compositions of protein fractions produced as described in Examples 6 and 7 are Compositions of protein fractions produced as described in Examples 6 and 7
- Phospholipoproteins were removed from cheese whey by microfiltration through a 1.4- ⁇ m membrane. 60 cm 3 of the whey so clarified were passed through 30 cm 3 of strong anion exchange resin Duolite A 101 (Rohm & Haas, France) regenerated into Cl'-form at a rate of 150 cm 3 /h at pH 5, 6, 7 and 8. At each pH, the whey was circulated through the resin for 30 min. The experiments were conducted at room temperature. After circulation, 100 cm 3 of ion-exchanged water were passed through the column, and the wash water was combined with the whey fraction (alpha-fraction). Protein attached to the column was eluted with 0.1 N HCl (beta-fraction).
- Duolite A101 virtually bound no protein, being thus unsuitable for protein fractionation.
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Abstract
Description
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Priority Applications (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP95905668A EP0757522A1 (en) | 1994-01-21 | 1995-01-20 | Process for fractionating whey proteins and the components so obtained |
AU14193/95A AU1419395A (en) | 1994-01-21 | 1995-01-20 | Process for fractionating whey proteins and the components so obtained |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FI940316A FI96090C (en) | 1994-01-21 | 1994-01-21 | Method for fractionation of whey proteins |
FI940316 | 1994-01-21 |
Publications (1)
Publication Number | Publication Date |
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WO1995019714A1 true WO1995019714A1 (en) | 1995-07-27 |
Family
ID=8539644
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/FI1995/000027 WO1995019714A1 (en) | 1994-01-21 | 1995-01-20 | Process for fractionating whey proteins and the components so obtained |
Country Status (4)
Country | Link |
---|---|
EP (1) | EP0757522A1 (en) |
AU (1) | AU1419395A (en) |
FI (1) | FI96090C (en) |
WO (1) | WO1995019714A1 (en) |
Cited By (13)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6096870A (en) * | 1994-01-05 | 2000-08-01 | Sepragen Corporation | Sequential separation of whey |
WO2001041580A1 (en) * | 1999-12-08 | 2001-06-14 | Fonterra Co-Operative Group Limited | Method of obtaining glyco-macro-peptide deplete product from whey |
EP1234507A1 (en) * | 2001-02-26 | 2002-08-28 | Wageningen Centre for Food Sciences | Process for isolating beta-lactoglobulin from milk or milk fractions |
WO2004067557A1 (en) * | 2003-01-31 | 2004-08-12 | Henkel Kommanditgesellschaft Auf Aktien | Methods for refining concentrated enzyme solutions |
US7018665B2 (en) | 1999-12-08 | 2006-03-28 | Massey University | Process for separation of whey proteins using a novel anion exchanger |
FR2889067A1 (en) * | 2005-07-29 | 2007-02-02 | Cie Laitiere Europ Soc En Comm | Using protein fraction from whey for control of body weight, e.g. to promote slimming, comprises beta-lactoglobulin and alpha-lactalbumin at specified ratio |
US7651716B2 (en) | 2001-12-21 | 2010-01-26 | Wyeth Llc | Methods for reducing adverse effects of feeding formula to infants |
WO2010037736A1 (en) * | 2008-09-30 | 2010-04-08 | Upfront Chromatography A/S | A METHOD FOR PROVIDING A β-LACTOGLOBULIN PRODUCT AND AN α-ENRICHED WHEY PROTEIN ISOLATE |
CN102590413A (en) * | 2012-01-18 | 2012-07-18 | 浙江省疾病预防控制中心 | Quantitative detection method for bovine alpha-lactalbumin |
US9055752B2 (en) | 2008-11-06 | 2015-06-16 | Intercontinental Great Brands Llc | Shelf-stable concentrated dairy liquids and methods of forming thereof |
WO2016023553A1 (en) * | 2014-08-15 | 2016-02-18 | Upfront Chromatography A/S | Method for separating alpha-lactalbumin and beta-lactoglobulin |
WO2016055064A3 (en) * | 2014-10-06 | 2016-06-09 | Upfront Chromatography A/S | Isolation of soluble proteins from aggregated casein-containing mixtures |
US11490629B2 (en) | 2010-09-08 | 2022-11-08 | Koninklijke Douwe Egberts B.V. | High solids concentrated dairy liquids |
-
1994
- 1994-01-21 FI FI940316A patent/FI96090C/en not_active IP Right Cessation
-
1995
- 1995-01-20 WO PCT/FI1995/000027 patent/WO1995019714A1/en not_active Application Discontinuation
- 1995-01-20 EP EP95905668A patent/EP0757522A1/en not_active Withdrawn
- 1995-01-20 AU AU14193/95A patent/AU1419395A/en not_active Abandoned
Non-Patent Citations (2)
Title |
---|
JOURNAL OF DAIRY SCIENCE, Volume 73, No. 9, 1990, SHIGERU YOSHIDA, "Isolation of beta-Lactoglobulin and alpha-Lactalbumin by Gel Filtration Using Sephacryl S-200 and Purification by Diethylaminoethyl Ion-Exchange Chromatography", page 2292 - page 2298. * |
MILCHWISSENSCHAFT, Volume 42, No. 11, 1987, A.R. HILL et al., "Quantification and Characterization of Whey Protein Fractions Separated by Anion Exchange Chromatography", page 693 - page 696. * |
Cited By (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6096870A (en) * | 1994-01-05 | 2000-08-01 | Sepragen Corporation | Sequential separation of whey |
WO2001041580A1 (en) * | 1999-12-08 | 2001-06-14 | Fonterra Co-Operative Group Limited | Method of obtaining glyco-macro-peptide deplete product from whey |
US7018665B2 (en) | 1999-12-08 | 2006-03-28 | Massey University | Process for separation of whey proteins using a novel anion exchanger |
EP1234507A1 (en) * | 2001-02-26 | 2002-08-28 | Wageningen Centre for Food Sciences | Process for isolating beta-lactoglobulin from milk or milk fractions |
US7651716B2 (en) | 2001-12-21 | 2010-01-26 | Wyeth Llc | Methods for reducing adverse effects of feeding formula to infants |
WO2004067557A1 (en) * | 2003-01-31 | 2004-08-12 | Henkel Kommanditgesellschaft Auf Aktien | Methods for refining concentrated enzyme solutions |
FR2889067A1 (en) * | 2005-07-29 | 2007-02-02 | Cie Laitiere Europ Soc En Comm | Using protein fraction from whey for control of body weight, e.g. to promote slimming, comprises beta-lactoglobulin and alpha-lactalbumin at specified ratio |
EP2801260A1 (en) * | 2008-09-30 | 2014-11-12 | Upfront Chromatography A/S | An alpha-enriched whey protein isolate |
WO2010037736A1 (en) * | 2008-09-30 | 2010-04-08 | Upfront Chromatography A/S | A METHOD FOR PROVIDING A β-LACTOGLOBULIN PRODUCT AND AN α-ENRICHED WHEY PROTEIN ISOLATE |
US9035031B2 (en) | 2008-09-30 | 2015-05-19 | Upfront Chromatography A/S | Method for providing a β-lactoglobulin product and an α-enriched whey protein isolate |
US9055752B2 (en) | 2008-11-06 | 2015-06-16 | Intercontinental Great Brands Llc | Shelf-stable concentrated dairy liquids and methods of forming thereof |
US11490629B2 (en) | 2010-09-08 | 2022-11-08 | Koninklijke Douwe Egberts B.V. | High solids concentrated dairy liquids |
CN102590413B (en) * | 2012-01-18 | 2013-12-25 | 浙江省疾病预防控制中心 | Quantitative detection method for bovine alpha-lactalbumin |
CN102590413A (en) * | 2012-01-18 | 2012-07-18 | 浙江省疾病预防控制中心 | Quantitative detection method for bovine alpha-lactalbumin |
WO2016023553A1 (en) * | 2014-08-15 | 2016-02-18 | Upfront Chromatography A/S | Method for separating alpha-lactalbumin and beta-lactoglobulin |
CN106793797A (en) * | 2014-08-15 | 2017-05-31 | 预层析股份有限公司 | The method for separating alpha-lactalbumin and beta lactoglobulin |
WO2016055064A3 (en) * | 2014-10-06 | 2016-06-09 | Upfront Chromatography A/S | Isolation of soluble proteins from aggregated casein-containing mixtures |
Also Published As
Publication number | Publication date |
---|---|
EP0757522A1 (en) | 1997-02-12 |
FI96090B (en) | 1996-01-31 |
AU1419395A (en) | 1995-08-08 |
FI940316A (en) | 1995-07-22 |
FI96090C (en) | 1996-05-10 |
FI940316A0 (en) | 1994-01-21 |
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