GB2055846A - Process for lowering the gelling temperature of whey proteins obtained from milk - Google Patents
Process for lowering the gelling temperature of whey proteins obtained from milk Download PDFInfo
- Publication number
- GB2055846A GB2055846A GB7923104A GB7923104A GB2055846A GB 2055846 A GB2055846 A GB 2055846A GB 7923104 A GB7923104 A GB 7923104A GB 7923104 A GB7923104 A GB 7923104A GB 2055846 A GB2055846 A GB 2055846A
- Authority
- GB
- United Kingdom
- Prior art keywords
- proteins
- temperature
- whey
- solution
- gelling
- Prior art date
- Legal status (The legal status 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 status listed.)
- Granted
Links
- 108010046377 Whey Proteins Proteins 0.000 title claims abstract description 48
- 238000000034 method Methods 0.000 title claims abstract description 38
- 235000021119 whey protein Nutrition 0.000 title claims abstract description 35
- 235000013336 milk Nutrition 0.000 title claims abstract description 10
- 239000008267 milk Substances 0.000 title claims abstract description 10
- 210000004080 milk Anatomy 0.000 title claims abstract description 10
- 235000018102 proteins Nutrition 0.000 claims abstract description 54
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 54
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 54
- 102000007544 Whey Proteins Human genes 0.000 claims abstract description 29
- 239000007864 aqueous solution Substances 0.000 claims abstract description 20
- 239000000243 solution Substances 0.000 claims abstract description 19
- 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
- 125000003396 thiol group Chemical group [H]S* 0.000 abstract description 9
- 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
- 239000012460 protein solution Substances 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
- 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
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
SPECIFICATION
Process for lowering the gelling temperature of whey proteins obtained from milk
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 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 by 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 900C to lower than 990C 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 600C 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 700C to effect an increase in the sulphydryle 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 700 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 effects 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 an 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 the 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 solution at a concentration of from 3 to 5% weight/volume.
It is essential that no precipitation, gelling or heat coagulation of the protein occurs. In general, to achieve this the pH of the solution needs to be slightly alkaline, for example from 7.5 to 9.
Preferably the pH is maintained at a level of substantially 8.0.
For normal procedures the temperature should in general be less than 900C 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 1 200C 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 elevated 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 900C or as long as 30 minutes at 700C.
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 850C. 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% or 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 of the order of 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 700C and 900C 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 obtaining 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: 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 900C for 30 seconds after which time, it was rapidly cooled in an ice,"vater 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 x 10 6 FI moles/g to 20 x 10-6 ,tt moles/g.
When a solution containing 15% weight/volume protein was prepared, a firm gel was formed at 250C whereas the unmodified whey protein required a temperature of 720C 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 800C for 3 minutes. As a result of this treatment the free sulphydryl content was increased to 8.0 x 1 0-6 /1 moles/g, and the gelling temperature was lowered to approximately 500C.
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 face sulphydryl content was increased to 9.0 x 10-6 !( moles/g. A 15% weight/volume aqueous solution of the treated proteins had a gelling temperature of 500 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 800C for 10 minutes. As a result of this treatment the free sulphydryl content was increased to 16.2 x 10-6 /t moles/g. A 15% weight/volume aqueous solution of the treated protein had a gelling temperature of 420C.
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 800C for 10 minutes. As a result of this treatment the free sulphydryl content was increased to 22 x 10-6 # moles/g. A 1 5% weight/volume aqueous solution of the treated protein had a gelling temperature of 360C.
By varying the parameters of concentration temperature and time a range of products can be prepared with gelling temperatures varying between 250C and 720C 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 from 0.5 to 10%
weight/volume at an elevated temperature of at
least 700C to effect an increase in the sulphydryle
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.
2. A process as claimed in claim 1 in which the
concentration of the proteins in the aqueous
solution is from 0.5% to 10% weight/volume.
3. A process as claimed in claim 2 in which the
concentration of proteins in the aqueous solution
is from 3% to 5% weight/volume.
4. A process as claimed in any of claims 1 to 3
in which the pH of the solution is from 7.5 to 9.
5. A process as claimed in claim 4 in which the
pH of the solution is substantially 8.
6. A process as claimed in any of claims 1 to 5
in which the temperature of the aqueous solution
is less than 900C.
7. A process as claimed in any of the preceding
claims in which the concentration of proteins in
the aqueous solution is substantially 3%
weight/volume.
8. A process as claimed in claim 7 in which the aqueous solution is maintained at an elevated temperature of from 700C to 900C for a period of from 30 seconds at 900C to 30 minutes at 700C
and proportional intermediate values.
9. A process as claimed in claim 8 in which the
aqueous solution is maintained at an elevated
temperature of from 7 50C to 850C for a period of
from 5 to 3 minutes.
10. A process as claimed in claim 1
substantially as hereinbefore described in any one
of the Examples.
Priority Applications (11)
| 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 |
| CA000353770A CA1148536A (en) | 1979-07-03 | 1980-06-11 | Process for lowering gelling temperature of whey proteins obtained from milk |
| AU59425/80A AU532195B2 (en) | 1979-07-03 | 1980-06-19 | Lowering gelling temp of whey obtained from milk |
| NL8003624A NL8003624A (en) | 1979-07-03 | 1980-06-23 | PROCESS FOR REDUCING THE GELTING TEMPERATURE OF WHEY PROTEINS OBTAINED FROM MILK. |
| IT49069/80A IT1145343B (en) | 1979-07-03 | 1980-06-25 | PROCEDURE FOR LOWERING THE TEMPERATURE OF GELIFICATION OF WHEY PROTEINS OBTAINED FROM MILK |
| JP8768680A JPS5626159A (en) | 1979-07-03 | 1980-06-27 | Lowering of gelating temperature of whey protein obtained from milk |
| DE19803024356 DE3024356A1 (en) | 1979-07-03 | 1980-06-27 | METHOD FOR REDUCING THE GEL TEMPERATURE OF MILK PROTEINS OBTAINED FROM MILK |
| IE1358/80A IE49694B1 (en) | 1979-07-03 | 1980-06-30 | Process for lowering gelling temperature of whey proteins obtained from milk |
| NZ194216A NZ194216A (en) | 1979-07-03 | 1980-07-02 | Process for lowering the gelling temperature of whey protein derived from milk |
| DK286380A DK286380A (en) | 1979-07-03 | 1980-07-02 | PROCEDURE FOR THE REDUCTION OF GELING TEMPERATURES FOR WHEEL PROTEINS MADE FROM MILK |
| FR8014855A FR2460630B1 (en) | 1979-07-03 | 1980-07-03 | PROCESS FOR LOWERING THE GELING TEMPERATURE OF BREASTFEED PROTEINS OBTAINED FROM MILK |
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 |
|---|---|
| GB2055846A true GB2055846A (en) | 1981-03-11 |
| GB2055846B GB2055846B (en) | 1983-02-23 |
Family
ID=10506261
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB7923104A Expired GB2055846B (en) | 1979-07-03 | 1979-07-03 | Process for lowering the 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) |
Cited By (7)
| 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 |
| WO1992020239A1 (en) * | 1991-05-16 | 1992-11-26 | Ault Foods Limited | Whey protein product method for its production and use thereof in foods |
| WO1993002567A2 (en) * | 1991-08-01 | 1993-02-18 | Ault Foods Limited | Whey and ice cream products and processes |
| US7166316B2 (en) | 2000-12-19 | 2007-01-23 | Nandi Proteins Limited | Fat replacement material and method of manufacture thereof |
| US8192780B2 (en) | 2006-03-23 | 2012-06-05 | Fonterra Co-Operative Group Limited | Dairy product and process |
| EP3484304B1 (en) | 2016-07-15 | 2020-09-02 | Arla Foods Amba | Method of producing concentrated or dried acid-gellable whey protein aggregates, and related compositions and food products |
| USD942586S1 (en) | 2018-11-27 | 2022-02-01 | Church & Dwight Co., Inc. | Front band on a spray nozzle |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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. |
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 JP JP8768680A patent/JPS5626159A/en active Granted
- 1980-06-27 DE DE19803024356 patent/DE3024356A1/en not_active Withdrawn
- 1980-06-30 IE IE1358/80A patent/IE49694B1/en unknown
- 1980-07-02 DK DK286380A patent/DK286380A/en not_active Application Discontinuation
- 1980-07-02 NZ NZ194216A patent/NZ194216A/en unknown
- 1980-07-03 FR FR8014855A patent/FR2460630B1/en not_active Expired
Cited By (9)
| 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 |
| WO1992020239A1 (en) * | 1991-05-16 | 1992-11-26 | Ault Foods Limited | Whey protein product method for its production and use thereof in foods |
| WO1993002567A2 (en) * | 1991-08-01 | 1993-02-18 | Ault Foods Limited | Whey and ice cream products and processes |
| WO1993002567A3 (en) * | 1991-08-01 | 1993-05-27 | Ault Foods | Whey and ice cream products and processes |
| US7166316B2 (en) | 2000-12-19 | 2007-01-23 | Nandi Proteins Limited | Fat replacement material and method of manufacture thereof |
| US8192780B2 (en) | 2006-03-23 | 2012-06-05 | Fonterra Co-Operative Group Limited | Dairy product and process |
| EP3484304B1 (en) | 2016-07-15 | 2020-09-02 | Arla Foods Amba | Method of producing concentrated or dried acid-gellable whey protein aggregates, and related compositions and food products |
| US11252977B2 (en) | 2016-07-15 | 2022-02-22 | Arla Foods Amba | Method of producing concentrated or dried acid-gellable whey protein aggregates, and related compositions and food products |
| USD942586S1 (en) | 2018-11-27 | 2022-02-01 | Church & Dwight Co., Inc. | Front band on a spray nozzle |
Also Published As
| Publication number | Publication date |
|---|---|
| CA1148536A (en) | 1983-06-21 |
| DE3024356A1 (en) | 1981-01-22 |
| IE49694B1 (en) | 1985-11-27 |
| GB2055846B (en) | 1983-02-23 |
| AU532195B2 (en) | 1983-09-22 |
| NL8003624A (en) | 1981-01-06 |
| DK286380A (en) | 1981-01-04 |
| JPH0150381B2 (en) | 1989-10-30 |
| IT8049069A0 (en) | 1980-06-25 |
| AU5942580A (en) | 1981-01-15 |
| JPS5626159A (en) | 1981-03-13 |
| FR2460630A1 (en) | 1981-01-30 |
| NZ194216A (en) | 1982-05-25 |
| FR2460630B1 (en) | 1985-07-12 |
| IE801358L (en) | 1981-01-03 |
| IT1145343B (en) | 1986-11-05 |
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| PCNP | Patent ceased through non-payment of renewal fee |