WO2007100264A1 - Produit laitier et procédé laitier - Google Patents

Produit laitier et procédé laitier Download PDF

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Publication number
WO2007100264A1
WO2007100264A1 PCT/NZ2006/000168 NZ2006000168W WO2007100264A1 WO 2007100264 A1 WO2007100264 A1 WO 2007100264A1 NZ 2006000168 W NZ2006000168 W NZ 2006000168W WO 2007100264 A1 WO2007100264 A1 WO 2007100264A1
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Prior art keywords
calcium
casein
fraction
alpha
sodium
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PCT/NZ2006/000168
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Inventor
Diane Joy Sinclair
Satyendra Parshu Ram
Lilian De Barros Ferreira
Christina June Coker
Peter Dudley Elston
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Fonterra Cooperative Group Ltd
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Fonterra Cooperative Group Ltd
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    • 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
    • A23J3/04—Animal proteins
    • A23J3/08—Dairy proteins
    • A23J3/10—Casein
    • 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; PREPARATION THEREOF
    • A23C19/00—Cheese; Cheese preparations; Making thereof
    • A23C19/02—Making cheese curd
    • A23C19/05—Treating milk before coagulation; Separating whey from curd
    • A23C19/053—Enrichment of milk with whey, whey components, substances recovered from separated whey, isolated or concentrated proteins from milk
    • 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; PREPARATION 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
    • 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
    • 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
    • A23L33/16—Inorganic salts, minerals or trace elements
    • A23L33/165—Complexes or chelates
    • 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
    • A23L33/19—Dairy proteins
    • 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 invention relates to casein fractions and processes for their preparation.
  • the invention also relates to dairy products enriched or depleted in particular casein fractions and processes for their preparation.
  • the products are useful as agents for altering the properties of simulated cheese products and other dairy compositions.
  • the fractions may also be used as a source of bioactive peptides or as a source of phosphopeptides for delivery of high levels of calcium.
  • Whole casein and casemate consist of four primary proteins - alpha sl -casein, alpha s2 -casein, beta- casein and kappa-casein. Each of these components, has a unique composition and structure.
  • the approximate content of the four proteins in casein/caseinate products is 36- 40, 10-12, 33-40 and 10-12 for alpha sl - 5 alpha s2 -, beta- and kappa-casein respectively.
  • Alpha s i -casein and alpha s2 -casein are the products of two different genes.
  • alpha s -casein refers to a mixture of the two proteins.
  • Hipp et al J Dairy Res 35, 272-281, 1952 refined the method of Warner (1944) and performed the fractionation of whole casein by one of two different methods.
  • a crude alpha s -casein precipitate was obtained by acidifying (to pH 6.5) an ethanolic solution of whole casein (50% ethanol/0.4 M ammonium acetate). The precipitate was redissolved in weak ammonia, diluted with water to 6% protein and the solution made 50% in ethanol.
  • Homogeneous purity alpha s -casein was claimed to be recovered by acidifying the solution to pH 7.2 with ammonium acetate.
  • Adjustment of the pH of whole casein dispersions in urea have also been used to precipitate the alpha s -casein. This has been achieved either by adjusting a 6.6 M urea solution of casein to pH 1.3-1.5 (Zittle & Custer, J Dairy Sci. 46, 1183-1188, 1963) or by adjusting a 3.3 M urea system to pH 4.5 (Fox & Guiney, J Dairy Sci. 39, 49-53, 1972).
  • the alpha s -casein fraction is readily precipitated from solution when calcium chloride is added. This observation was used to advantage in a wide range of methods described for the isolation of the alpha s -casem fraction.
  • the aim has generally been either to prepare highly purified samples of alpha s -casein (especially free of kappa-casein) or to prepare samples of highly purified kappa-casein (free of alpha s -casein and beta-casein).
  • Kudo (NZ J Dairy Sci Tech 15, 245-254 1980) developed a solvent based precipitation in which n-propanol was used to remove the alpha s2 -casein fraction from a dispersion of whole casein at pH 6.5; the alphas-casein fraction, present in the supernatant (which contained 40% w/v n- propanol), was subsequently recovered by the addition of calcium.
  • the further purification of the products was achieved by (both) repeated extractions and chromatography on DEAE- cellulose exchangers (see Kudo, 1980 for details).
  • polycations have been used to complex the alpha s -casein fraction at high pH.
  • This complex is precipitated by acidifying the alkaline caseinate mixture to pH 5.8 (or 8.0) and the alpha s -casein product is subsequently recovered by alkaline extraction of the precipitate.
  • DEAE-dextran has been shown to be effective for this purpose (see Gurov et al, J Dairy Sci 64, 380-383, 1981 for details).
  • JP 54-95768 relates to a process which comprises cooling an alkaline metal salt solution of casein having a process concentration of 0.5 to 6% and a pH of 7 to 10 to 0 to 15°C and adding a divalent cation followed by the removal of the resulting alpha s -casein precipitate from the remaining solution.
  • JP 59-91849 relates to a method characterized by the addition of a divalent salt to a casein fraction containing alpha s - and beta-casein as major ingredients at a temperature of 0-10°C and fractionating this into separate fractions, one of which has alpha s -casein as a major ingredient and the other having beta-casein as a major ingredient.
  • US Patent 5,068,118 describes a process for separating whole casein into its components and includes the steps of dissolving whole casein in an aqueous urea solution having a urea concentration sufficient to provide the solution, reducing the urea concentration of the solution to about 4.6 molar by addition of water, removing precipitated alpha s -casein, reducing the urea concentration of the remaining solution to about 1.7 molar by addition of water, removing precipitated beta-casein and then precipitating gamma-casein present in the remaining solution.
  • the invention provides a method for the preparation of an alpha s -casein fraction comprising:
  • the dairy feedstock is selected from the group comprising UF concentrated cheese milks, total milk proteins, milks or milk protein solutions previously diafiltered or dialysed or electrodialysed or ion exchanged for the removal of minerals, micellar casein preparations, UF concentrates of acidified cheese milks, skim milk, milk and other milk products having at least 40% of the milk protein as casein.
  • the feedstock may be a liquid dairy stream or it may be reconstituted from a dried product.
  • the feedstock comprises at least 60% casein, more preferably at least 80%
  • the cation exchanger is loaded with sodium and exchanges calcium in the feedstock for sodium.
  • the feedstock is whey-depleted.
  • the feedstock is selected from a milk (including skim milk) and a milk protein concentrate, preferably whey-depleted.
  • a milk including skim milk
  • a milk protein concentrate preferably whey-depleted.
  • alpha s -casein fraction refers to a fraction comprising casein in which the ratio of alpha s -casein to beta-casein is at least 30% higher, preferably at least 60% higher, most preferably 100% higher than the material before fractionation
  • beta-casein fraction refers to a fraction comprising casein in which the ratio of beta- casein to alpha s -casein is at least 30% higher, preferably at least 60% higher, most preferably 100% higher than the material before fractionation
  • whey-depleted milk includes “whey depleted whole milk” and "whey-depleted skim milk”.
  • whey-depleted means that relative to the corresponding product when not “whey-depleted” the level of whey proteins is at least 10%, preferably at least 20%, more preferably at least 50%, lower.
  • a whey-depleted milk is obtainable by microf ⁇ ltration of a milk that is not whey-depleted.
  • milk protein concentrate refers to a milk protein product in which greater than 55% and preferably greater than 70%, more preferably 75% of the dry matter is milk protein.
  • An MPC may be prepared fresh or may be a dried product for reconstitution with water, milk or another suitable aqueous liquid.
  • milk protein isolate refers to a milk protein product in which at least 85% of the dry matter is milk protein.
  • An MPI may be prepared fresh or may be a dried product for reconstitution with water, milk or another suitable aqueous liquid.
  • total milk protein refers to a milk protein product that is an MPC or MPI in which the whey protein is denatured.
  • the starting material is whey-depleted sldm milk retentate.
  • milk is microfiltered at low pH (pH range 4.9-7.5, preferably 5.5-6.3, most preferably pH 5.8-6.1) in order to enhance calcium reduction while whey proteins are removed into the permeate.
  • Membranes e.g. of MWCO having pore size between 0.1-0.8 microns are preferred.
  • the preferred temperature for this step is in the range 4-60°C, more preferably 10- 50 0 C 5 most preferably 40-50°C).
  • An alternative starting material is an MPC or MPI without whey-depletion, preferably with at least 70%, more preferably 75%, more preferably at least 80%, most preferably at least 85% of the total solids as protein.
  • the MPC is prepared by ultrafiltration at a pH in the range of 4.9-7.5 preferably 5.5-6.5, most preferably 5.8-6.1.
  • the pH is adjusted to 4.9-7.5, preferably 5.5-6.3, most preferably 5.8-6.1.
  • the preferred ion exchanger is a cation exchanger bearing strongly acidic groups in the sodium form or potassium form.
  • acidic groups are sulphonic acid groups.
  • One preferred ion exchange resin is IMAC HP 11 IE manufactured by Rohm & Haas. This resin has a divinylbenzene copolymer matrix.
  • the functional groups are sulphonic acid groups that can be obtained in the Na+ form.
  • Another preferred ion exchanger is Amberlite SRlL.
  • step (c) The cation exchange step allows better precipitation in step (c).
  • anion exchange step Following the cation exchange step, it is preferred to use an anion exchange step.
  • the anion exchange may be in the Cl or OH form.
  • the anion exchanger bears weak basic groups e.g. primary, secondary or tertiary amines.
  • a preferred ion exchanger is Purelite Al 035.
  • the cation-exchange and anion-exchange steps are carried out at the same time using a mixed bed of the two ion-exchange resins.
  • anion exchange step is preferred because it allows cleaner separation of alpha s -casein from the beta-casein and kappa casein fraction. This is currently believed to be due to removal of phosphate ions. Use of this step is particularly advantageous when the starting material is an MPC.
  • the calcium-depleted whey-depleted material may be subjected to concentration, preferably ultrafiltration or ultrafiltration with diafiltration.
  • concentration preferably ultrafiltration or ultrafiltration with diafiltration.
  • concentration could be carried out using rennet treatment or acidification. In this step lactose and ash is (further) reduced.
  • the (heat-treated) calcium-depleted material is preferably diluted to give a casein concentration of 2- 10%, preferably 4-7%.
  • the preferred temperature for the calcium precipitation step is 0-25°C, preferably 1-15°C, more preferably 4-10°C, most preferably 4-8°C.
  • the concentrated calcium-depleted material may be cooled before or during calcium precipitation.
  • the cooling time used is typically 5-200 minutes, preferably 30-200 minutes, more preferably 30-60 minutes.
  • Calcium is preferably added as a soluble calcium salt or as the hydroxide, more preferably as a calcium salt.
  • Preferred salts include the chloride, acetate, ascorbate, citrate, lactate and tartrate salts. Calcium chloride is currently the most preferred.
  • the calcium salt may be added as either a powder or as a solution.
  • Salts of other nutrient metal ions may be added before or with the calcium addition step. These may be selected from potassium, magnesium, manganese, zinc, chromium, copper and molybdenum salts. Potassium, magnesium, manganese and zinc are preferred for this purpose. Inclusion of such salts will result in binding of these salts to the casein molecules so that the eventual product will act as a source of these nutrients.
  • a soluble calcium salt is added with or following the addition of a soluble phosphate salt (for example a sodium phosphate salt).
  • a soluble phosphate salt for example a sodium phosphate salt. This allows formation of a calcium- alpha s -casein-phosphate complex.
  • the alpha s -deplete-casein stream remaining in solution is rich in beta-casein and kappa-casein.
  • the flocculated alpha s -casein may be collected for example by sedimentation or centrifugation at (e.g. at 2,000-15,000 x g for 10 min).
  • the alpha s -casein fraction is preferably separated from the supernatant fraction by cold centrifugation.
  • the precipitate may be minced in a colloid mill and have its pH adjusted to pH 4.2-5.2, preferably 4.6-4.9.
  • the calcium content may be adjusted by washing the precipitate with acidified water until a desired level of calcium has been reached.
  • the precipitated and washed alpha s -casein fraction may be converted to a sodium or potassium alpha s -caseinate.
  • the pH of the precipitate is adjusted to 6.0-7.0, preferably 6.5-7.0 at 50-60°C and blended with another dairy stream such as MPC or a cream.
  • the precipitate may also be re-dissolved in water at pH 6.0-7.0 at 5°C-85°C, preferably 16°C-60°C more preferably 16°C -3O 0 C.
  • the alpha-casein product or blended product may then be concentrated (for example by evaporation) and dried (for example by spray drying).
  • the pH of the protein material undergoing ion exchange treatment is in the range of pH 5 to pH 9.5, more preferably 5.5-6.5, most preferably 5.7-6.0.
  • the preferred pH for carrying out the calcium precipitation of alpha s -casein is pH 6.5 to pH 10.5, preferably 8.5-10.5, most preferably 9.5-10.3.
  • Especially preferred is pH 9.8-10.2.
  • the preferred concentration of calcium for use in precipitating the alpha s -casein from the calcium-depleted whey-depleted MPC is 0.4-8% (w/w), preferably 1-8% (w/w), more preferably 2-8% (w/w), most preferably 4-6% w(Ca)/w(protein).
  • the preferred concentrations are 5-200 mM, preferably 30-80 mM when the level of protein is between 2% and 4%. Mild agitation may be usefully employed during this step.
  • Alpha s -casein produced by the above method is particularly useful as a process cheese ingredient. It can be blended into other dairy product streams to make fresh alpha enriched products or cheese milks, or converted into dry ingredients (eg caseinates, MPC or total milk protein products) for use in functional or nutraceutical foods. Caseinates can be prepared using ion exchange on a cation exchanger charged with potassium or sodium or by addition of KOH or NaOH.
  • the alpha s -casein ingredient after separation from the fraction containing high beta-casein and kappa-casein may be adjusted to have high, medium or low calcium, 2500-6500 mg/100g, 1000- 2500 mg/100 g or 0.5-1000 mg calcium per 100 g product respectively.
  • the freshly precipitated alpha s -casein is high in calcium but where a low or medium calcium product is required, calcium can be removed, for example by dialysis.
  • the traction with higher beta-casein and high kappa-casein may be recovered by the usual method used for casein recovery, e.g. by renneting or by acid precipitation, or alternatively by dialysis or ultrafiltration followed by e.g. spray drying.
  • the calcium content of that fraction may be adjusted to provide low (0.5-100 mg calcium/100 g product), medium (100-1500 mg calcium/100 g product) or high calcium (greater than 1500 mg calcium per lOOg product) as described for alpha s -casein.
  • the precipitated and washed fraction with higher beta-casein, high kappa-casein may be used to enrich another dairy product stream or may be converted to a sodium or potassium beta/kappa-caseinate.
  • the high beta-casein, high kappa-casein fraction may be used for a variety of purposes including as a source of glycomacropeptide for enhanced nutrition, and a source of bioactive peptides, and as a source of protein for infant formula.
  • an alpha s -casein fraction prepared by the method of the invention.
  • the invention provides a method for the preparation of a beta-casein fraction comprising:
  • Steps (a)-(d) are preferably carried out as described above in relation to the preferred embodiments for preparation of the alpha s -casein.
  • the removal of the precipitated fraction may be achieved for example by sedimentation or by centrifugation (e.g. at 2,000-15,000 x g for 10 min).
  • the protein component of the unprecipitated fraction recovered may be obtained by the usual method used for casein recovery, e.g. by renneting or by acid precipitation, or alternatively by dialysis or ultrafiltration followed by e.g. spray drying.
  • the preferred methods of carrying out steps (a) - (c) are as for the preparation of the alpha s -casein fraction.
  • both the precipitated fraction and the unprecipitated fraction are recovered to provide both an alpha s -casein fraction and a beta-casein fraction.
  • the beta-casein fraction will generally also contain kappa-casein.
  • beta-casein fraction prepared by the method of the invention.
  • the invention also provides a method of making a sodium or sodium/calcium caseinate product comprising the steps of:
  • This process may be manipulated to allow production of casemates with desired mineral profiles. For example, requirements can be met to provide particular Ca/Mg mineral mixtures.
  • the process can be used to provide sodium potassium mixtures for food functional applications, new MPCs 5 total milk proteins and milk compositions for cheese manufacture.
  • Preferred cation exchangers are as described for the methods for preparing alpha s -casein and beta-casein.
  • Preferred microfiltration methods are as described above.
  • the resulting caseinate is useful as an intermediate for producing alpha s -casein or beta-casein. It may be used directly or spray dried for future use.
  • Figure 1 is a schematic drawing of a preferred embodiment of the process for preparing casein fractions.
  • Figure 2 is a schematic drawing of a preferred embodiment of the process for preparing casein fractions.
  • Figure 3 is a schematic drawing of a preferred embodiment of the process for preparing casein fractions.
  • Skim milk 25 L, casein to whey ratio of 3.2 was fractionated by batch microfiltration to a VCF of 2.1 at 50°C (using the MFSl unit from Alpha Laval fitted with 0.1 ⁇ m membrane).
  • the retentate was diafiltered twice (13.6 L water addition each time) to further remove whey proteins, lactose and minerals.
  • a lO L sample of the diafiltered retentate (casein: whey ratio of 9.1, 5.57% protein) was passed twice through a cation exchange resin (Rohm & Haas Amberlite SRlL Na form (bed volume 4L) to fully substitute sodium for calcium as the counterion associated with the protein in solution.
  • the breakthrough Prior to the second pass through the cation exchange resin, the breakthrough was adjusted from pH 8.2 to pH 6.1 with HCl.
  • the breakthrough (calcium depleted, sodium form of the proteinate) was recovered (4% w/v protein), was cooled to 7°C, and adjusted to a pH of between 10.0-10.43 using 10% NaOH.
  • Calcium chloride (74.04 g) was added to 10 L of the breakthrough, the mixture stirred and left at 5°C overnight.
  • the flocculated protein was recovered by centrifugation (30 min, 10000 rpm with rotor J14 at 8°C).
  • the sedimented protein (885 g) was slurried in 200 mL of water and acidulated to pH 4.93 with HCl. This acidulated mixture was left in the cold room held at 4°C overnight and the protein recovered by centrifugation and freeze-dried.
  • the alpha s -casein to beta-casein ratio in skim milk and standard lactic casein is 1:0.94.
  • the preparation above had an alpha s -casein to beta-casein ratio of 1.81 : 1.
  • Beta casein can be recovered from the liquid fraction by the standard methods used for the recovery of casein, namely adjusting the pH of the liquid to pH 4.6 using a mineral acid (typically 2 M HCl) and heating at 45°C-47°C followed by recovery of the precipitate by centrifugation.
  • the liquid stream may be concentrated by ultrafiltering with a 10 K Dalton membrane, and the concentrated protein is then spray dried.
  • MPI milk protein isolate, 85% milk protein, Fonterra
  • the pH adjusted solution was passed twice through a one litre bed of cation exchange resin (Amberlite SRlL Na form, Rohm & Haas) to fully substitute sodium for calcium as the counterion associated with the protein in solution.
  • the breakthrough (calcium depleted, sodium form of the proteinate) was recovered, was cooled to below 10°C, diluted to 2-3% casein and adjusted to a pH of 10.5 using 10% NaOH.
  • Calcium chloride was added to 100 mL aliquots of the breakthrough (1.25, 1.50, 1.75 and 2.00 mL of 43% CaCl 2 .2H 2 O per 100 mL aliquot). The mixtures were stirred and held at 4°C overnight.
  • the flocculated protein was recovered by centrifugation (10 min, 8000 rpm with rotor J14 at 8 0 C).
  • the chilled precipitates were diluted 1/20 using alkali urea buffer and subjected to alkaline urea polyacrylaminde gel electrophoresis to separate the caseins prior to staining with Amido Black and analysing using densitometry.
  • the alpha s -casein to beta-casein ratio in skim milk and standard lactic casein is 1 :0.94.
  • Each preparation above had an alpha s -casein to beta-casein ratio in the range 1.47-1.59.1
  • MPC milk protein concentrate, 70% milk protein, Fonterra 200 g was mixed with 180OmL of water at 50 0 C 5 chilled to 4°C and adjusted to pH 5.95 with 10% HCl.
  • the pH adjusted solution was passed twice through a one litre bed of cation exchange resin
  • the breakthrough was diluted to 2-3% casein and adjusted to a pH of 10.5 using 10% NaOH.
  • the chilled precipitates were diluted 1/20 using alkali urea buffer and subjected to alkaline urea polyacrylamide gel electrophoresis to separate the caseins prior to staining with Amido Black and analysing using densitometry.
  • the alphas-casein to beta-casein ratio in skim milk and standard lactic casein is 1:0.94.
  • the precipitate had alpha s -casein to beta-casein ratios of 3.7, 13.9, 7.88 and 6.9 for addition of 1.25, 1.50, 1.75 and 2.00 mL of the calcium chloride solution respectively.
  • Skim milk 34 L, casein to whey ratio of 3.2 was adjusted in pH to 6.0 by addition of 5% NaOH. It was then fractionated by batch microfiltration to a VCF of 3 at 10 0 C (using the MFSl unit from Alpha Laval fitted with 0.1 ⁇ m membrane). The retentate was diafiltered twice (16 L water addition each time) to further remove whey proteins, lactose and minerals. A 2 L sample of the diafiltered retentate (8-10% total solids) was passed twice through a cation exchange resin (Rohm & Haas Amberlite SRlL Na form (bed volume 1 litre)) to fully substitute sodium for calcium as the counterion associated with the protein in solution.
  • a cation exchange resin Roshm & Haas Amberlite SRlL Na form (bed volume 1 litre)
  • the breakthrough (calcium depleted, sodium form of the proteinate) was recovered (5.7 w/w protein of which 5.5% was casein), diluted to 2-3% casein, cooled to 7°C, and adjusted to a pH of 10.5 using 10% NaOH.
  • To six 600 mL aliquots of calcium chloride was added (1.25 mL, 1.35 mL, 1.5 mL, 1.7 mL, 2.0 mL and 2.5 mL of 43% CaG 2 .2H 2 O). The mixtures were stirred for 3 minutes with a glass rod.
  • the precipitated protein was recovered by centrifugation (30 min, 8000 rpm with rotor J14 at 8°C).
  • the precipitated protein was diluted 1/20 into alkali urea buffer and subjected to alkali urea polyacrylamide gel electrophoresis to separate the caseins prior to staining with Amido Black and analysing using densitometry.
  • the alpha s -casein to beta-casein ratio was 3.4, 3.2, 3.2, 3.2, 3.1 and 2.8
  • MPC70 powder (Fonterra, milk protein concentrate 70% protein, 20kg) was reconstituted to 5% total solids with water at 50°C and adjusted to pH 6.00 with 5% HCl.
  • the pH adjusted solution was processed in a UFS4 with continuous diafiltration until the protein level was 85% of total solids.
  • Ultrafiltration retentate (2.5 L) was diluted to 10% total solids.
  • the pH was adjusted to pH 5.9.
  • the retentate was then passed through a cation exchange resin (Amberlite SRlL, Na form, Rohm and Haas bed volume IL) to remove calcium.
  • the breakthrough (calcium depleted, sodium form of the proteinate) was recovered and divided into 3 portions. One portion was diluted to 2% casein. The second was diluted to 3% casein and the third to 4% casein. Each portion was cooled to below 10°C and then the portions were split as shown in Table 1.
  • the alpha s -casein to beta-casein ratio in skim milk and standard lactic casein as measured by densitometry is 1 :0.94.
  • Table 1 shows the alpha s -casein to beta-casein ratios obtained.
  • MPC 70 milk protein concentrate, 70% milk protein, Fonterra 250 g was mixed with water at 50 0 C to form a reconstituted MPC 70 with 5% total solids, chilled to 4°C and adjusted to pH 6.0 with 5% HCl.
  • the pH adjusted material was subjected to diafiltration in a 4 loop ultrafitration system with 5-10 K Dalton membranes in continuous mode until the permeate was less than 0.5° Brix and less than 0.8mS/cm conductivity.
  • the pH was adjusted to pH 5.9 with 5% HCl.
  • a portion of the pH adjusted solution was passed twice through a 125 litre bed of cation exchange resin (Amberlite SRlL Na form, Rohm & Haas) (first cycle 900L, recharged with sodium, second cycle 1068L, 200L not used) to fully substitute sodium for calcium as the counterion associated with the protein in solution.
  • the breakthrough (calcium depleted, sodium form of the proteinate) was recovered, cooled to below 1O 0 C, diluted to 4% casein and adjusted to a pH of 10.0 using 10% NaOH.
  • the remaining portion of the diafiltered material was not subjected to ion exchange and was diluted to 4% casein.
  • the material subjected to calcium depletion can show variations in protein concentration and pH
  • the method of calcium depletion can be varied
  • the percentage calcium depletion and percentage whey depletion can also be varied.

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  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Polymers & Plastics (AREA)
  • Health & Medical Sciences (AREA)
  • Nutrition Science (AREA)
  • Biochemistry (AREA)
  • Mycology (AREA)
  • Zoology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Inorganic Chemistry (AREA)
  • Dairy Products (AREA)
  • Peptides Or Proteins (AREA)

Abstract

La présente invention concerne un procédé pour la préparation d'une fraction de caséine alpha S comprenant : (a) d'obtenir un échantillon liquide d'un produit laitier de départ comprenant de la caséine constituant au moins 40 % en poids des protéines du lait ; (b) de mettre en contact le produit laitier de départ avec un échangeur de cations chargé de sodium ou de potassium ou des deux pour remplacer le calcium par le sodium ou le potassium ou les deux ; (c) d'ajouter du calcium au lait ou concentré de protéines du lait appauvri en calcium résultant ; et (d) de récupérer la fraction précipitée. L'invention concerne également un procédé servant à préparer une fraction de caséine bêta comprenant les étapes (a)-(c) ci-dessus et (d) d'enlever la fraction précipitée et de récupérer la fraction non précipitée. Entre autres utilisations, on peut utiliser la fraction de caséine alpha S pour ajuster la texture d'un produit de type fromage.
PCT/NZ2006/000168 2005-06-30 2006-06-30 Produit laitier et procédé laitier Ceased WO2007100264A1 (fr)

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NZ54102105 2005-06-30
NZ541021 2005-06-30

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WO2007100264A1 true WO2007100264A1 (fr) 2007-09-07

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Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2008063089A1 (fr) * 2006-11-23 2008-05-29 Fonterra Co-Operative Group Limited Produit laitier et procédé
WO2009108074A1 (fr) * 2008-02-29 2009-09-03 Christina June Coker Gel à base de protéines de lait
WO2010140905A1 (fr) * 2009-06-04 2010-12-09 Fonterra Co-Operative Group Limited Fromage fondu fortifie au calcium sans sels emulsifiants, et son procede de preparation
WO2014068187A1 (fr) * 2012-10-31 2014-05-08 Valio Ltd Fromage fondu et sa préparation
EP2866576A4 (fr) * 2012-06-20 2016-09-07 Univ Massey Procédé d'enrichissement en minéraux et ses utilisations
AU2015218429B2 (en) * 2012-06-20 2017-08-31 Société des Produits Nestlé S.A. Micronutrient Fortification Process and its Uses
WO2022190045A1 (fr) 2021-03-11 2022-09-15 Fonterra Co-Operative Group Limited Produit laitier et procédé
US11470857B2 (en) 2013-01-23 2022-10-18 Arla Foods Amba Method of producing beta-casein compositions and related products

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WO2003003847A1 (fr) * 2001-07-06 2003-01-16 Hannah Research Institute Procedes permettant d'extraire des fractions de caseine du lait et de caseinates et production de nouveaux produits

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WO2003003847A1 (fr) * 2001-07-06 2003-01-16 Hannah Research Institute Procedes permettant d'extraire des fractions de caseine du lait et de caseinates et production de nouveaux produits

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Cited By (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2008063089A1 (fr) * 2006-11-23 2008-05-29 Fonterra Co-Operative Group Limited Produit laitier et procédé
EP2262375A4 (fr) * 2008-02-29 2014-03-19 Fonterra Co Operative Group Gel à base de protéines de lait
JP2011512816A (ja) * 2008-02-29 2011-04-28 フォンテラ コ−オペレイティブ グループ リミティド 乳タンパク質ゲル
CN102164497A (zh) * 2008-02-29 2011-08-24 方塔拉合作集团有限公司 乳蛋白凝胶
WO2009108074A1 (fr) * 2008-02-29 2009-09-03 Christina June Coker Gel à base de protéines de lait
WO2010140905A1 (fr) * 2009-06-04 2010-12-09 Fonterra Co-Operative Group Limited Fromage fondu fortifie au calcium sans sels emulsifiants, et son procede de preparation
CN102573505A (zh) * 2009-06-04 2012-07-11 方塔拉合作集团有限公司 无乳化盐的钙强化再制干酪及其制备方法
EP2866576A4 (fr) * 2012-06-20 2016-09-07 Univ Massey Procédé d'enrichissement en minéraux et ses utilisations
AU2015218429B2 (en) * 2012-06-20 2017-08-31 Société des Produits Nestlé S.A. Micronutrient Fortification Process and its Uses
WO2014068187A1 (fr) * 2012-10-31 2014-05-08 Valio Ltd Fromage fondu et sa préparation
US11470857B2 (en) 2013-01-23 2022-10-18 Arla Foods Amba Method of producing beta-casein compositions and related products
WO2022190045A1 (fr) 2021-03-11 2022-09-15 Fonterra Co-Operative Group Limited Produit laitier et procédé
US12310382B2 (en) 2021-03-11 2025-05-27 Fonterra Co-Operative Group Limited Dairy product and process

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