IE49694B1 - Process for lowering gelling temperature of whey proteins obtained from milk - Google Patents
Process for lowering gelling temperature of whey proteins obtained from milkInfo
- Publication number
- IE49694B1 IE49694B1 IE1358/80A IE135880A IE49694B1 IE 49694 B1 IE49694 B1 IE 49694B1 IE 1358/80 A IE1358/80 A IE 1358/80A IE 135880 A IE135880 A IE 135880A IE 49694 B1 IE49694 B1 IE 49694B1
- Authority
- IE
- Ireland
- Prior art keywords
- proteins
- temperature
- solution
- whey
- gelling
- Prior art date
Links
- 108010046377 Whey Proteins Proteins 0.000 title claims abstract description 48
- 238000000034 method Methods 0.000 title claims abstract description 37
- 235000021119 whey protein Nutrition 0.000 title claims abstract description 35
- 235000013336 milk Nutrition 0.000 title claims abstract description 9
- 239000008267 milk Substances 0.000 title claims abstract description 9
- 210000004080 milk Anatomy 0.000 title claims abstract description 9
- 235000018102 proteins Nutrition 0.000 claims abstract description 53
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 53
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 53
- 102000007544 Whey Proteins Human genes 0.000 claims abstract description 30
- 239000000243 solution Substances 0.000 claims abstract description 20
- 239000007864 aqueous solution Substances 0.000 claims abstract description 18
- 125000003396 thiol group Chemical group [H]S* 0.000 claims abstract description 11
- 230000000694 effects Effects 0.000 claims abstract description 8
- 238000005345 coagulation Methods 0.000 claims abstract description 7
- 230000015271 coagulation Effects 0.000 claims abstract description 7
- 238000001556 precipitation Methods 0.000 claims abstract description 7
- 238000006243 chemical reaction Methods 0.000 claims abstract description 4
- 238000001816 cooling Methods 0.000 claims abstract description 4
- 239000012460 protein solution Substances 0.000 claims description 7
- 239000005862 Whey Substances 0.000 description 13
- 230000004048 modification Effects 0.000 description 11
- 238000012986 modification Methods 0.000 description 11
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 235000013351 cheese Nutrition 0.000 description 4
- 235000014103 egg white Nutrition 0.000 description 4
- 210000000969 egg white Anatomy 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 102000035118 modified proteins Human genes 0.000 description 4
- 108091005573 modified proteins Proteins 0.000 description 4
- 239000005018 casein Substances 0.000 description 3
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
- 235000021240 caseins Nutrition 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 235000016709 nutrition Nutrition 0.000 description 3
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 239000001828 Gelatine Substances 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 230000000704 physical effect Effects 0.000 description 2
- 238000001694 spray drying Methods 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 108010068370 Glutens Proteins 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 150000008044 alkali metal hydroxides Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000002301 combined effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000004945 emulsification Methods 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 235000006486 human diet Nutrition 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 230000008719 thickening Effects 0.000 description 1
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
- A23J3/04—Animal proteins
- A23J3/08—Dairy proteins
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Dairy Products (AREA)
Abstract
Process for lowering the gelling temperature of whey protein derived from milk comprises maintaining an aqueous solution of such whole whey proteins having a concentration of proteins of from 0.5 to 10% weight/volume at an elevated temperature of at least 70 DEG C to effect an increase in the sulphydryl groups available for reaction, the period of time over which the proteins are maintained at the elevated temperature and the pH of the solution both being selected such that precipitation, gelling and coagulation of the proteins whilst at the elevated temperature is prevented, and cooling the resultant solution.
Description
The present invention relates to a process for lowering the gelling temperature of whey proteins obtained from milk, especially casein whey or cheese whey.
Proteins are essential to the human diet because of their 5 ability to provide essential amino acids. However, many proteins are also used for their physical properties as well as their nutritional properties, in food systems where a gelling, foaming, emulsification or thickening function may be required and these properties are often collectively known as the functional properties of a protein.
Casein, egg white, gelatine and gluten are all examples of proteins that are used for their functional properties, rather than their nutritional properties. During recent years a great deal of work has been directed towards recovery of proteins from milk whey and whereas the nutritional superiority of whey proteins is undisputed, the functional use of whey protein has been limited because of the poor physical properties of commercial products. Methods are now commercially available whereby whey products containing up to 90% or more whey protein may be produced, but these products tend to be rather limited in their functional use, since the whipping and gelling properties are generally inferior to those of egg white, and whole egg, and the viscosity properties are inferior to those of casein, gelatine or soya.
The whole whey proteins are globular proteins and are capable of being utilised in a functional manner. The specific functional properties of whey proteins in commercial products however, are at a level which, at the present time do not, in general, compare favourably with equivalent functional properties of proteins derived from other sources.
It has been proposed to effect a controlled breakdown of whey proteins into peptides and amino-acids hy hydrolysis at a particular pH level whereby to improve the whipping properties of such proteins. Such a process, however, has been found to have a deleterious effect on the gelling properties of such proteins.
It has also been proposed to increase the whipping properties of aqueous solutions containing dissolved cheese whey protein especially cheese whey protein concentrates obtained by gel filtration of partially delactosed cheese whey by heating the aqueous protein solution to a temperature within the range of from at least 90°C to lower than 99°C for not more than about 5 minutes and preferably for about 0.1 minute at a pH of from 5 to 8.5, preferably 6 to 7.5 and cooling the solution to below 60°C and whipping the aqueous solution within about 8 hours after heating. The aqueous solutions thus produced are stated however not to be suitable for replacement of egg whites used in food systems requiring the heat-set or coagulation property of egg whites.
It is an object of the present invention to provide a process whereby the gelling properties of whey proteins may be modified such that the temperature at which gelling thereof occurs is lower than that of the unmodified proteins.
It has now been found that the structure of whey proteins can be modified such that interaction between the modified protein molecules occurs at a lower temperature than between unmodified protein molecules thus causing a lowering in the gelling temperature of the proteins. It has been found that this modification occurs if the proteins are held at an elevated temperature for a sufficient time whilst the pH of the system is maintained at a level which prevents precipitation coagulation or gelling of the protein during the time the proteins are maintained at the elevated temperature.
According to the present invention a process is provided for lowering the gelling temperature of whey protein derived from milk which comprises maintaining an aqueous solution of such whole whey proteins having a concentration of proteins of from 0.5 to 10% weight/volume at an elevated temperature of at least 70°C and at an alkaline pH to effect an increase in the sulphydryl groups available for reaction, the period of time over which the proteins are maintained at the elevated temperature and the pH of the solution both being selected such that precipitation, gelling and coagulation of the proteins whilst at the elevated temperature is prevented, and cooling the resultant solution.
For the modification to occur within a reasonable time the temperature must be maintained at or above 70°C. For a given degree of modification of the proteins the temperature and duration of the treatment are inter-related, in general the higher the temperature the shorter the period of time required, and the lower the temperature the longer the period required. The temperature should be high enough to effect the necessary modification but not high enough or be maintained for a sufficiently long period that it effect coagulation, precipitation or the extensive breaking of primary structure peptide bonds although S-S or other labile bonds, within the protein molecules may be ruptured.
The effect of the above modification process on the protein molecules is to open out the protein molecules and thereby bring into a reactable state one or more of any internal SH or S-S groups which *
in the natural condition of the protein molecules are enclosed within the protein molecule and unavailable for reaction. It is believed that opening up of the protein molecules also causes an increase in the disulphide groups which are available for interaction with sulphydryl groups in other protein molecules and that this does play at least some part in the lowering of the gelling temperature which results.
It is believed that the extra sulphydryl groups and extra disulphide groups rendered accessible, enable interaction of the protein molecules to be increased and the gelling temperature thereby decreased.
The modification treatment is effected on the proteins in solution i.e. in aqueous solution. The concentration of the proteins in the aqueous solution may be from 0.5 to 10« weight/volume.
Below 0.5« concentration the solution may be uneconomical to process. Above 10« concentration it would be difficult or impossible to prevent uncontrolled interaction of the protein molecules, leading to insolubilisation, precipitation or even gelling in the processing equipment. Preferably, the proteins are present in the aqueous
49894 solution at a concentration of from 3 to 52 weight/volume.
It is essential that no precipitation, gelling or heat coagulation of the protein occurs. To achieve this the pH of the solution is maintained slightly alkaline, for example from 7.5 to 9.
Preferably the pH is maintained at a level of 8.0.
For normal procedures the temperature should in general be less than 90°C to enable workable time periods to be achieved. If ultra high temperature techniques are used, however, much shorter times are feasible and temperatures as high as 120°C or more may be possible.
The period over which the elevated temperature must be maintained for a given degree of modification, i.e. a given lowering in the gelling temperature, is also dependent on the concentration of the proteins in the aqueous solution. For any given elevation temperature, the lower the concentration the longer the period of time required at that elevated temperature to effect a given degree of modification.
Thus using non-ultra high temperature techniques the time required for a 3% weight/volume concentration of whey protein can be as short as 30 seconds at 90°C or as long as 30 minutes at 70°C. Preferably, for a 3% concentration weight/volume of whey proteins the temperatures and other parameters should be chosen to provide a dwell time at the elevated temperature of from about 3 to 5 minutes. Generally this can be achieved by using a temperature between 75 and 85°C. At concentrations below 3% weight/volume longer times would be necessary at a given temperature for the same degree of modification and at concentrations greater than 3% e.g. 5% to 10%, shorter times will in general be necessary for a given temperature to achieve the same modification.
The modification process of the present invention can be effected on unconcentrated milk whey but is preferably effected on whey which has been subjected to an ultrafiltration treatment. Preferably the process of the invention is carried out on concentrated separated whey in which the protein concentration is from 3% to 5% weight/volume most preferably 3% weight/volume. A fractionated milk whey may also be used but if the fractionation is taken too far some individual fractions may not respond to the process. Care should be exercised however, in any concentration or fractionation technique employed to avoid subjecting the proteins to elevated temperatures which might cause denaturation of the proteins particularly where concentrates from different sources are to be used.
In a preferred method of carrying out the process of the invention, a milk whey having a protein concentration of about 3% weight/volume has its pH adjusted to about pH 8.0 using a dilute alkali metal hydroxide solution such as sodium hydroxide. The temperature of the whey is then raised to between 70°C and 90°C for a residence time of between 30 minutes and 30 seconds either in a continuous manner by means of heat exchangers or using a batchwise technique. At the end of the appropriate residence time the whey is rapidly cooled and optionally the pH may be adjusted to 6.5 to 7.0 and the whey then concentrated and dried to yield a dry modified whey protein. Low temperature concentration and spray drying from fairly dilute solutions should be effected to avoid any denaturation of the proteins by such techniques.
Analysis of modified whey proteins produced by the method of the invention has shown that the available sulphydryl content has been increased over that obtained in the unmodified whey proteins. Determination of the gelling temperature of reconstituted unmodified and modified protein solutions containing 15% weight/volume of protein has shown that the modified protein gells at a lower temperature but that there is no significant decrease in the gel strength as between a gel produced from unmodified protein and a gel produced from modified protein.
The degree of lowering in the gelling temperature will depend on the combined effect of temperature and dwell time for a given concentration of whey proteins in the aqueous solution being treated. For a given concentration of whey protein and a given temperature of treatment, the lowering in gelling temperature is greater with increasing time and for a given concentration of whey proteins and a given time the lowering in the gelling temperature is greater the higher the temperature.
The invention will be further illustrated by reference to the following examples:20 EXAMPLE 1
A whey protein concentrate powder prepared by an ultrafiltration and low temperature spray drying technique (containing 85% protein,
8.5% fat and 3% lactose) was reconstituted in water to give a solution containing 3% protein. The pH of this solution was adjusted to pH 8.0 using dilute sodium hydroxide and the temperature of the solution increased to 90°C for 30 seconds after which time, it was rapidly cooled in an ice/water bath. The solution was then dried by means of a spray drier. Analysis of the dried product showed that the sulphydryl content had increased from 2 χ 10® μ moles/g to 20 x 10”®μ moles/g. When a solution containing 15% weight/volume protein was prepared, a firm gel was formed at 25°C whereas the unmodified whey protein required a temperature of 72°C before a firm gel would form.
EXAMPLE 2
The procedure described in Example 1 was repeated except that the whey protein solution was held at 80°C for 3 minutes.
As a result of this treatment the free sulphydryl content was increased to 8.0 x 10~®μ moles/g, and the gelling temperature was lowered to approximately 50°C.
EXAMPLE 3
The procedure of Example 1 was repeated except that the whey protein solution had a concentration of 1% weight/volume and was held at 80°C for 10 minutes. As a result of this treatment the free sulphydryl content was increased to
9.0 x 10% moles/g. A 15% weight/volume aqueous solution of the treated proteins had a gelling temperature of 50°C.
EXAMPLE 4
The procedure of Example 1 was repeated except that the whey protein solution had a concentration of 5% weight/volume and was held at 80°C for 10 minutes. As a result of this treatment the free sulphydryl content was increased to 16.2 χ 10θμ moles/g.
A 15% weight/volume aqueous solution of the treated protein had a gelling temperature of 42°C.
EXAMPLE 5
The procedure of Example 1 was repeated except that the whey protein solution had a concentration of 10% weight/volume and was held at 80°C for 10 minutes. As a result of this treatment the free sulphydryl content was increased to 22 x 10 ® μ moles /g.
A 15% weight/volume aqueous solution of the treated protein had a gelling temperature of 36°C.
By varying the parameters of concentration temperature and time a range of products can be prepared with gelling temperatures varying between 25°C and 72°C thus greatly increasing the number of applications and the efficiency with which the whey proteins could be used in food systems. Furthermore products having consistent gelling temperatures and gelling strength become possible. The product produced by the method of the invention can of course be used in admixture with untreated whey proteins or with materials from other sources.
Claims (10)
1. A process for lowering the gelling temperature of whey protein derived from milk which comprises maintaining an aqueous solution of such whole whey proteins having a concentration of proteins of 5 from 0.5 to 10% weight/volume at an elevated temperature of at least 70°C and at an alkaline pH to effect an increase in the sulphydryl groups available for reaction, the period of time over which the proteins are maintained at the elevated temperature and the pH of the solution both being selected such that precipitation, gelling 10 and coagulation of the proteins whilst at the elevated temperature is prevented, and cooling the resultant solution.
2. A process as claimed in claim 1, which concentration of proteins in the aqueous solution is from 3% to 5% weight/volume.
3. A process as claimed in claim 1 or 2 in which the pH of the 15 solution is from 7.5 to 9.
4. A process as claimed in claim 3 in which the pH of the solution is 8.
5. A process as claimed in any of claims 1 to 4 in which the temperature of the aqueous solution is less than 90°C. 20
6. A process as claimed in any of the preceding claims in which the concentration of proteins in the aqueous solution is 3% weight/volume.
7. A process as claimed in claim 6 in which the aqueous solution is maintained at an elevated temperature of from 70°C to 90°C 25 for a period of from 30 seconds at 90°C to 30 minutes at 70°C and proportional intermediate values.
8. A process as claimed in claim 7 in which the aqueous solution is maintained at an elevated temperature of from 75°C to 85°C for a period of from 5 to 3 minutes.
9. A process as claimed in claim 1 substantially as hereinbefore 5 described in any one of the Examples.
10. A whey protein solution when produced by a process as claimed in any of the preceding claims.
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB7923104A GB2055846B (en) | 1979-07-03 | 1979-07-03 | Process for lowering the gelling temperature of whey proteins obtained from milk |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IE801358L IE801358L (en) | 1981-01-03 |
| IE49694B1 true IE49694B1 (en) | 1985-11-27 |
Family
ID=10506261
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE1358/80A IE49694B1 (en) | 1979-07-03 | 1980-06-30 | Process for lowering gelling temperature of whey proteins obtained from milk |
Country Status (11)
| Country | Link |
|---|---|
| JP (1) | JPS5626159A (en) |
| AU (1) | AU532195B2 (en) |
| CA (1) | CA1148536A (en) |
| DE (1) | DE3024356A1 (en) |
| DK (1) | DK286380A (en) |
| FR (1) | FR2460630B1 (en) |
| GB (1) | GB2055846B (en) |
| IE (1) | IE49694B1 (en) |
| IT (1) | IT1145343B (en) |
| NL (1) | NL8003624A (en) |
| NZ (1) | NZ194216A (en) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4675201A (en) * | 1979-11-19 | 1987-06-23 | Ciba Corning Diagnostics Corp. | Protein composition characterized by lower thermogelation temperature and improved acid solubility |
| JPS58129696U (en) * | 1982-02-25 | 1983-09-02 | ミクロエンヂニヤリング株式会社 | Electronic component adhesive tape |
| JPH0687748B2 (en) * | 1986-05-19 | 1994-11-09 | 明治乳業株式会社 | Whey-Protein Modification Method |
| JPS646272U (en) * | 1987-06-29 | 1989-01-13 | ||
| JPH075217B2 (en) * | 1989-07-24 | 1995-01-25 | ローム株式会社 | Device for folding the hoop material |
| JP2529052B2 (en) * | 1991-01-25 | 1996-08-28 | 雪印乳業株式会社 | Whey protein-containing solution, whey protein gel product using the same, whey protein powder, and processed food |
| FR2672471B1 (en) * | 1991-02-08 | 2000-12-01 | PROCESS FOR INSTANT THERMAL COAGULATION OF A COAGULABLE PROTEIN AT ISOELECTRIC PH, SUCH AS A CASEIN, BY LOWERING THE ALKALINE ION CONTENT. | |
| CA2046741C (en) * | 1991-05-16 | 1999-06-29 | Yashavantkumar Jayasinh Asher | Whey protein concentrate and its use in ice cream |
| WO1993002567A2 (en) * | 1991-08-01 | 1993-02-18 | Ault Foods Limited | Whey and ice cream products and processes |
| GB0030926D0 (en) | 2000-12-19 | 2001-01-31 | Univ Heriot Watt | Fat replacement product and process for its manufacture |
| AR060076A1 (en) | 2006-03-23 | 2008-05-21 | Fonterra Co Operative Group | DAIRY PRODUCT AND ITS PROCESS |
| DK3484304T3 (en) | 2016-07-15 | 2020-12-07 | Arla Foods Amba | PROCEDURE FOR THE MANUFACTURE OF CONCENTRATED OR DRIED ACID-ADJUSTABLE WHEAT PROTEIN UNITS AND RELATED COMPOSITIONS AND FOOD PRODUCTS |
| USD942586S1 (en) | 2018-11-27 | 2022-02-01 | Church & Dwight Co., Inc. | Front band on a spray nozzle |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3935323A (en) * | 1973-12-06 | 1976-01-27 | Stauffer Chemical Company | Process for improving whipping properties of aqueous protein solutions |
-
1979
- 1979-07-03 GB GB7923104A patent/GB2055846B/en not_active Expired
-
1980
- 1980-06-11 CA CA000353770A patent/CA1148536A/en not_active Expired
- 1980-06-19 AU AU59425/80A patent/AU532195B2/en not_active Ceased
- 1980-06-23 NL NL8003624A patent/NL8003624A/en not_active Application Discontinuation
- 1980-06-25 IT IT49069/80A patent/IT1145343B/en active
- 1980-06-27 DE DE19803024356 patent/DE3024356A1/en not_active Withdrawn
- 1980-06-27 JP JP8768680A patent/JPS5626159A/en active Granted
- 1980-06-30 IE IE1358/80A patent/IE49694B1/en unknown
- 1980-07-02 NZ NZ194216A patent/NZ194216A/en unknown
- 1980-07-02 DK DK286380A patent/DK286380A/en not_active Application Discontinuation
- 1980-07-03 FR FR8014855A patent/FR2460630B1/en not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| GB2055846A (en) | 1981-03-11 |
| IT1145343B (en) | 1986-11-05 |
| FR2460630B1 (en) | 1985-07-12 |
| AU532195B2 (en) | 1983-09-22 |
| DE3024356A1 (en) | 1981-01-22 |
| CA1148536A (en) | 1983-06-21 |
| NL8003624A (en) | 1981-01-06 |
| GB2055846B (en) | 1983-02-23 |
| FR2460630A1 (en) | 1981-01-30 |
| JPS5626159A (en) | 1981-03-13 |
| JPH0150381B2 (en) | 1989-10-30 |
| NZ194216A (en) | 1982-05-25 |
| IE801358L (en) | 1981-01-03 |
| AU5942580A (en) | 1981-01-15 |
| DK286380A (en) | 1981-01-04 |
| IT8049069A0 (en) | 1980-06-25 |
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