CA1148536A - Process for lowering gelling temperature of whey proteins obtained from milk - Google Patents
Process for lowering gelling temperature of whey proteins obtained from milkInfo
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- CA1148536A CA1148536A CA000353770A CA353770A CA1148536A CA 1148536 A CA1148536 A CA 1148536A CA 000353770 A CA000353770 A CA 000353770A CA 353770 A CA353770 A CA 353770A CA 1148536 A CA1148536 A CA 1148536A
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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
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- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Dairy Products (AREA)
Abstract
I
ABSTRACT
"PROCESS FOR LOWERING THE GELLING TEMPERATURE OF WHEY
PROTEINS OBTAINED FROM MILK"
The process of the invention relates to 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 70°C 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 precipit-ation, gelling and coagulation of the proteins whilst at the elevated temperature is prevented, and cooling the resultant solution.
ABSTRACT
"PROCESS FOR LOWERING THE GELLING TEMPERATURE OF WHEY
PROTEINS OBTAINED FROM MILK"
The process of the invention relates to 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 70°C 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 precipit-ation, gelling and coagulation of the proteins whilst at the elevated temperature is prevented, and cooling the resultant solution.
Description
~ SCRIP~?IO~
"~CESS ~OR IOWERL~G l!HE OEILING q~E~ERATU~E OF W~
.
PRO~EINS OB~AINED ~ROM MI~En.
The present invention relates to a pro¢ess for lowering the gelling temperature of whey proteins obtained from milk, especially casein whey or cheese whey.
Eroteins are es~ential to the human diet because of their ability to provide essential amino acids.
However, ma~y proteins are al~o used for their physical properties as well as their nutritional properties, in food systems where a gelling, foaming, emulsirication or thickening function may be required and these properties aro often collectively known as the functional proporties Or a protein. Casein, egg white, gelatine and ~luten are all examples Or proteins that are used ror their functional properties, rather than the~r nutritional properties. During recent years a ersat d~al Or wor~ has been directed towards reco~ery of ~rotein~ Srom milk whey and whereas the nutritional ~uperiority of whey proteins is undisputed, the ~unctional use Or whey protein has been limited because o~ the poor physical propérties of commercial product~.
Methods are now commercially a~ailable whereb~ whey products containing up to 9~% or more whey protein may - be produced, but these products tend to be rather limited in their functional u~e, since the whipping and gelling _properties are generally inferior to those of egg white, .~ ~
J
`
~ 1~853G
and whole egg, and the viscosity properties are inferior to thoqe o~ casein, gelatine or ~oya.
~ he whole whey proteins are globular protein~
and are capable of being utilised in a functional mannor. ~he #pecific functional properties of whey proteins in commer~ial products however, are at a level which, at the present time do not, in general, comp~re favourably with equivalent ~unctional propertie~ of protein~ derived from othcr ~ource~.
It has besn proposed to effect a controlled break-down of whey proteins into peptides and amino-acids by ~ydrolysi~ at a particular pH level whereby to improve the whipping properties of such protein~q. &ch a process, howevsr, has been found to have a deleteriou~
errect on the gelling properties of such proteins.
It has also been proposed to increase tho whipp~ng properties Or aqueous solutions containing di~sol~ed ch~ese whey prote~n e~poc~ally chee~e whey protein ~oncentratos obtained b~ gel filtration Or partially delactosed cheese whey by heating the aqueouR protein ~olution to a temperature within the range of from at lea~t 90~ to lower than 99C for not more tha~ about 5 minute~ and prererably for about 0.1 minute at a pH
Or from 5 to 8.5~ preferably 6 to 7.5 and cooling the 801ution to below 60C ~nd whipping the aqueous solution within about 8 hours after heati~g. ~he aqueous 1148S3~
solutions thus produced are stated however not to be suit-able 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.
lG 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 suf-ficient 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 there is provided 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 70C and at an 1148S3~
alkaline pH 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 pre-cipitation, gelling and coagulation of the proteins while at the elevated temperature is prevented, and cooling the resultant solution to a temperature at which no further change in the protein occurs.
For the modification to occur within a reasonable time the temperature must be maintained at or above 70C. For a given degree of modification of the proteins the temper-ature 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 break-ing 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 2s 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 `
~8536 i8 belie~ed that the opening up of the protein molecules also cauqes an increase i~ the di~ulphide groups which are available for interaction with sulph~dryl group~
in other protein molecules and that this does play at lcast some part in the lowering Or the gelling temperature which result~. It is believed that the extra sulphydryl groups and extra disulphide groups rendered accessible, enable interaction of the protein ~lecule~ to be ;ncrea~ed and the gelling temperature thereby decreased.
The modification treatment is effected on the protei~s in ~olution i.e. in aqueous solution. ~he ¢oncentration 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.
~bove 10% concentration it would be difficult or impossible to prevent uncontrolled interaction o~ the protein molecules, leading to insolubilisation, precipitation or e~en gelling in the proce~sing equipment. Preferably, the proteins are present in the aqueous ~olution at a concentratio~ of from ~ 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 8Ø
For normal procedure~ the temperature should in general be les~ than 90C to enable workable time period~
to be achieYed. If ultra high temperature techniques are used, howe~er, much ~horter times are feasible and tomperatures as high as 120C or more may be possible.
The period o~er which the elevated temperature must be maintained for a given degree of modification, i.e. a given lowering in the gellIng temperature, is also dependant on the conc~ntration of the protein~
in the aqueous solution~ For any given elevated temperature, the lower the concentration the longer the ~eriod of time required at that eleYated temperature to ~fect a given degree o~ modifi¢ation. ~hus using ~on-ultra high temperature techniques the time re~uired ~or a 3% weight/~olume con¢entration of whey proteIn ¢an be as short as 30 soconds at 90C or as long as 30 ~inutes at 70C. Preferabl~, ~or a 3% concontration wei pt/~olume of whey proteins the temperatures a~d other paramoters should be chosen to pro~ide a dwoll time at tho ele~ated temperature Or from about 3 to 5 minutes~ Generally thi~ can be achie~ed by using a temperature between 75 and 85C. ~t ¢on¢entrations below 3% weight/Yolume longer times would be necessary at a gi~en temperature for the same de OEee Or modification and at concentrations greater than 3% e.g. 5~ or 10%, shorter times will in ge~eral be necessary for a give~
temperatt~re to achie~e the same modif;cation.
11~853 The modification process of the present inve~tio~
can be effected on unconcentrated milk whey but i~
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 i5 of the order of 3% weight/volume. A fractionated milk whey may also be used but if the fractionation i8 taken too far ~c~e individual fraction~ may not re~pond to the process.
Care should be exercised however, ~n any concentration or fractionation technigue employed to avoid subjecting the proteins to olevated temperatures which might cau~e denaturation of the protein~ particularly where concentrates ~rom dif~erent sources are to be used.
In a prsferred method of carrying out the process Or the invention, a milX whey ha~ing a protein concen-tration of about 3% weight/volume has its p~ ad~sted to about pH 8.0 u~ing a dilute alkali metal hydroxide colution 8uch as sodium hydro2ide. ~he temperature of the whey is then raised to between 70C and 90C for a re~idence time of between 30 m;m~tes and 30 seconds e'ither i~ a continuous manner by means of heat exchangers or u~ing a batchwise technique. ~t the end of the appropriate re~idence time the whey i~ rapidly cooled an,d optionally the p~ may be adJusted to 6.5 to 7.0 a~d the whey then concentrated and dried to yield a dry modified whey protein. Iow temperature concentra~ion and ~8536 ~pray drying from fairî~ dilute solutions should be ef*ected to avoid any denaturation of the proteins by such tech~iques.
~ nalysis of modified whey proteins produced by the 5 method of the invention has shown that the available 8ulphydryl content has been increased over that obtaining in the unmodified whey proteins. Determination Or the gelling temperature of reconstituted unmodified and mo~ified protein solutions containing 15% weight/~olume 10 of protein has shown that the modified protein gells at a lower temperature but that there is no sign~ficant decrease in the gel strength as between a gel produ¢ed ~rom unmodi~ied protein and a gel produced from modified protein.
The degree of lowering in the gelling temperature will depend on the combined effect of temperature a~d dwell time for a given concentration of whey pro~ei ~ tho aqueou~ solution being treated. For a given con¢entration of whey protein and a given temperature of 20 treatment, the lowering in gelling temperature i8 OEeater with increasing time and for a give~ concen-tration of whe~ proteins and a given time the lowering in the gelling temperature i8 greater the hi~her the temperature.
~he in~ention will be further illu~trated by reference to the following examples -_ 9 _ F~4~D~LE 1.
~ whey protein concentrate powder prepared by an ultrafiltration and low temperature spra~ drying technique (containing 85% protein, 8.~% fat and 3%
5 lactose) was reconstituted in water to give a ~olution containing 3% protein. ~he pH of this solution was ad~usted to p~ 8.0 using dilute sodium hydroxide and the temperature of the solution increased to 90C for 30 se~onds after which time, it was rapidly cooled in a~
10 i~e/water bath. ~he solution was then dried by means of a spray drier. ~nalysis of the dried product showed that the sulphydryl content had i~creased from 2 x 10 6 moles ~g to 20 x 10-6~ moles /g. When a solution ¢ontaining 15% weight/~olume protein was prepared, a 15 firm gel was formed at 25C whereas the llnmodified whey protein required a temper~ture o~ 72C berore a rirm gel would form.
} 2, Tho procedure described in Example 1 wa~ repe~ted, 20 except that the whey protein solution was held at 80C
for 3 minutes. As a result of this treatment the ~ree ~ulphydryl content was increased to 8.0 x 10 6j~ mole~/g, ~nd the gelling temperature wa~ lowered to approxImately 50C.
25 EXAMEIE 3.
~ he procedure of Example 1 was repeated except that the whey protein solution had a concentration of 1~
~1~8536 weight/volume and wa~ held at 80C for 10 minutes. As a result of this treatment thè face sulph~dryl co~tent was increased to 9.0 x 10 6~ moles/g. A 15% weight/
volume aqueous solution of the treatod proteins had a gelling temperature of ~0C.
E~MPLE 4.
~ he procedure of Example 1 was repeated except that the whey protein solution had a concentration o~ 5% woight/volume and was held at 80C for 10 minutes.
10 ~s a result of this treatment the free ~ulphydryl content wa~ increased to 16.2 x 10-6ju moles/g. A 15% weight/
volume aqueous solution of the treated protein had a gelling temperature of 42C.
The procedure of Example 1 was repeated except that the whey prote~n solution had a concentration of 10% weight/Yolume and was held at 80C for 10 mi~utes.
~8 a rosult o~ this treatment tho freo sulphydryl content Wa8 increased to 22 x 10 6~ moles/g. ~ 15% weight/
20 volume aqueous solution of the treated protein had a gelling temperature of 36C.
By ~arying the parameters of concentration temperaturo and time a range of product3 can be prepared with gelling temperature~ varying between 25C and 72C thu~
25 greatly increasing the number of applications and the efficiency with which the whey proteins could be used in food systems. Further~ore product~ having consist.ent ~ ' t.
~8536 _11-gelling temperatures and gelling strength become possible.
The product produced ~y the method of the in~entio~ can of course be used in admixture with untreated whe~
protoins or with materials from other sources.
"~CESS ~OR IOWERL~G l!HE OEILING q~E~ERATU~E OF W~
.
PRO~EINS OB~AINED ~ROM MI~En.
The present invention relates to a pro¢ess for lowering the gelling temperature of whey proteins obtained from milk, especially casein whey or cheese whey.
Eroteins are es~ential to the human diet because of their ability to provide essential amino acids.
However, ma~y proteins are al~o used for their physical properties as well as their nutritional properties, in food systems where a gelling, foaming, emulsirication or thickening function may be required and these properties aro often collectively known as the functional proporties Or a protein. Casein, egg white, gelatine and ~luten are all examples Or proteins that are used ror their functional properties, rather than the~r nutritional properties. During recent years a ersat d~al Or wor~ has been directed towards reco~ery of ~rotein~ Srom milk whey and whereas the nutritional ~uperiority of whey proteins is undisputed, the ~unctional use Or whey protein has been limited because o~ the poor physical propérties of commercial product~.
Methods are now commercially a~ailable whereb~ whey products containing up to 9~% or more whey protein may - be produced, but these products tend to be rather limited in their functional u~e, since the whipping and gelling _properties are generally inferior to those of egg white, .~ ~
J
`
~ 1~853G
and whole egg, and the viscosity properties are inferior to thoqe o~ casein, gelatine or ~oya.
~ he whole whey proteins are globular protein~
and are capable of being utilised in a functional mannor. ~he #pecific functional properties of whey proteins in commer~ial products however, are at a level which, at the present time do not, in general, comp~re favourably with equivalent ~unctional propertie~ of protein~ derived from othcr ~ource~.
It has besn proposed to effect a controlled break-down of whey proteins into peptides and amino-acids by ~ydrolysi~ at a particular pH level whereby to improve the whipping properties of such protein~q. &ch a process, howevsr, has been found to have a deleteriou~
errect on the gelling properties of such proteins.
It has also been proposed to increase tho whipp~ng properties Or aqueous solutions containing di~sol~ed ch~ese whey prote~n e~poc~ally chee~e whey protein ~oncentratos obtained b~ gel filtration Or partially delactosed cheese whey by heating the aqueouR protein ~olution to a temperature within the range of from at lea~t 90~ to lower than 99C for not more tha~ about 5 minute~ and prererably for about 0.1 minute at a pH
Or from 5 to 8.5~ preferably 6 to 7.5 and cooling the 801ution to below 60C ~nd whipping the aqueous solution within about 8 hours after heati~g. ~he aqueous 1148S3~
solutions thus produced are stated however not to be suit-able 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.
lG 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 suf-ficient 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 there is provided 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 70C and at an 1148S3~
alkaline pH 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 pre-cipitation, gelling and coagulation of the proteins while at the elevated temperature is prevented, and cooling the resultant solution to a temperature at which no further change in the protein occurs.
For the modification to occur within a reasonable time the temperature must be maintained at or above 70C. For a given degree of modification of the proteins the temper-ature 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 break-ing 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 2s 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 `
~8536 i8 belie~ed that the opening up of the protein molecules also cauqes an increase i~ the di~ulphide groups which are available for interaction with sulph~dryl group~
in other protein molecules and that this does play at lcast some part in the lowering Or the gelling temperature which result~. It is believed that the extra sulphydryl groups and extra disulphide groups rendered accessible, enable interaction of the protein ~lecule~ to be ;ncrea~ed and the gelling temperature thereby decreased.
The modification treatment is effected on the protei~s in ~olution i.e. in aqueous solution. ~he ¢oncentration 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.
~bove 10% concentration it would be difficult or impossible to prevent uncontrolled interaction o~ the protein molecules, leading to insolubilisation, precipitation or e~en gelling in the proce~sing equipment. Preferably, the proteins are present in the aqueous ~olution at a concentratio~ of from ~ 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 8Ø
For normal procedure~ the temperature should in general be les~ than 90C to enable workable time period~
to be achieYed. If ultra high temperature techniques are used, howe~er, much ~horter times are feasible and tomperatures as high as 120C or more may be possible.
The period o~er which the elevated temperature must be maintained for a given degree of modification, i.e. a given lowering in the gellIng temperature, is also dependant on the conc~ntration of the protein~
in the aqueous solution~ For any given elevated temperature, the lower the concentration the longer the ~eriod of time required at that eleYated temperature to ~fect a given degree o~ modifi¢ation. ~hus using ~on-ultra high temperature techniques the time re~uired ~or a 3% weight/~olume con¢entration of whey proteIn ¢an be as short as 30 soconds at 90C or as long as 30 ~inutes at 70C. Preferabl~, ~or a 3% concontration wei pt/~olume of whey proteins the temperatures a~d other paramoters should be chosen to pro~ide a dwoll time at tho ele~ated temperature Or from about 3 to 5 minutes~ Generally thi~ can be achie~ed by using a temperature between 75 and 85C. ~t ¢on¢entrations below 3% weight/Yolume longer times would be necessary at a gi~en temperature for the same de OEee Or modification and at concentrations greater than 3% e.g. 5~ or 10%, shorter times will in ge~eral be necessary for a give~
temperatt~re to achie~e the same modif;cation.
11~853 The modification process of the present inve~tio~
can be effected on unconcentrated milk whey but i~
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 i5 of the order of 3% weight/volume. A fractionated milk whey may also be used but if the fractionation i8 taken too far ~c~e individual fraction~ may not re~pond to the process.
Care should be exercised however, ~n any concentration or fractionation technigue employed to avoid subjecting the proteins to olevated temperatures which might cau~e denaturation of the protein~ particularly where concentrates ~rom dif~erent sources are to be used.
In a prsferred method of carrying out the process Or the invention, a milX whey ha~ing a protein concen-tration of about 3% weight/volume has its p~ ad~sted to about pH 8.0 u~ing a dilute alkali metal hydroxide colution 8uch as sodium hydro2ide. ~he temperature of the whey is then raised to between 70C and 90C for a re~idence time of between 30 m;m~tes and 30 seconds e'ither i~ a continuous manner by means of heat exchangers or u~ing a batchwise technique. ~t the end of the appropriate re~idence time the whey i~ rapidly cooled an,d optionally the p~ may be adJusted to 6.5 to 7.0 a~d the whey then concentrated and dried to yield a dry modified whey protein. Iow temperature concentra~ion and ~8536 ~pray drying from fairî~ dilute solutions should be ef*ected to avoid any denaturation of the proteins by such tech~iques.
~ nalysis of modified whey proteins produced by the 5 method of the invention has shown that the available 8ulphydryl content has been increased over that obtaining in the unmodified whey proteins. Determination Or the gelling temperature of reconstituted unmodified and mo~ified protein solutions containing 15% weight/~olume 10 of protein has shown that the modified protein gells at a lower temperature but that there is no sign~ficant decrease in the gel strength as between a gel produ¢ed ~rom unmodi~ied protein and a gel produced from modified protein.
The degree of lowering in the gelling temperature will depend on the combined effect of temperature a~d dwell time for a given concentration of whey pro~ei ~ tho aqueou~ solution being treated. For a given con¢entration of whey protein and a given temperature of 20 treatment, the lowering in gelling temperature i8 OEeater with increasing time and for a give~ concen-tration of whe~ proteins and a given time the lowering in the gelling temperature i8 greater the hi~her the temperature.
~he in~ention will be further illu~trated by reference to the following examples -_ 9 _ F~4~D~LE 1.
~ whey protein concentrate powder prepared by an ultrafiltration and low temperature spra~ drying technique (containing 85% protein, 8.~% fat and 3%
5 lactose) was reconstituted in water to give a ~olution containing 3% protein. ~he pH of this solution was ad~usted to p~ 8.0 using dilute sodium hydroxide and the temperature of the solution increased to 90C for 30 se~onds after which time, it was rapidly cooled in a~
10 i~e/water bath. ~he solution was then dried by means of a spray drier. ~nalysis of the dried product showed that the sulphydryl content had i~creased from 2 x 10 6 moles ~g to 20 x 10-6~ moles /g. When a solution ¢ontaining 15% weight/~olume protein was prepared, a 15 firm gel was formed at 25C whereas the llnmodified whey protein required a temper~ture o~ 72C berore a rirm gel would form.
} 2, Tho procedure described in Example 1 wa~ repe~ted, 20 except that the whey protein solution was held at 80C
for 3 minutes. As a result of this treatment the ~ree ~ulphydryl content was increased to 8.0 x 10 6j~ mole~/g, ~nd the gelling temperature wa~ lowered to approxImately 50C.
25 EXAMEIE 3.
~ he procedure of Example 1 was repeated except that the whey protein solution had a concentration of 1~
~1~8536 weight/volume and wa~ held at 80C for 10 minutes. As a result of this treatment thè face sulph~dryl co~tent was increased to 9.0 x 10 6~ moles/g. A 15% weight/
volume aqueous solution of the treatod proteins had a gelling temperature of ~0C.
E~MPLE 4.
~ he procedure of Example 1 was repeated except that the whey protein solution had a concentration o~ 5% woight/volume and was held at 80C for 10 minutes.
10 ~s a result of this treatment the free ~ulphydryl content wa~ increased to 16.2 x 10-6ju moles/g. A 15% weight/
volume aqueous solution of the treated protein had a gelling temperature of 42C.
The procedure of Example 1 was repeated except that the whey prote~n solution had a concentration of 10% weight/Yolume and was held at 80C for 10 mi~utes.
~8 a rosult o~ this treatment tho freo sulphydryl content Wa8 increased to 22 x 10 6~ moles/g. ~ 15% weight/
20 volume aqueous solution of the treated protein had a gelling temperature of 36C.
By ~arying the parameters of concentration temperaturo and time a range of product3 can be prepared with gelling temperature~ varying between 25C and 72C thu~
25 greatly increasing the number of applications and the efficiency with which the whey proteins could be used in food systems. Further~ore product~ having consist.ent ~ ' t.
~8536 _11-gelling temperatures and gelling strength become possible.
The product produced ~y the method of the in~entio~ can of course be used in admixture with untreated whe~
protoins or with materials from other sources.
Claims (11)
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 70°C and at an alkaline pH 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 precipit-ation, gelling and coagulation of the proteins while at the elevated temperature is prevented, and cooling the result-ant solution to a temperature at which no further change in the protein occurs.
2. A process as claimed in claim 1 in which the concen-tration of whole whey proteins in the aqueous solution is from 3% to 5% weight volume.
3. A process as claimed in claim 1 in which the pH of the aqueous solution is from 7.5 to 9Ø
4. A process as claimed in claim 3 in which the pH of the aqueous solution is about 8.
5. A process as claimed in claim 1 in which the temperature of the aqueous solution is maintained below 90°C.
6. A process as claimed in claim 1 in which the concen-tration of whole whey proteins in the aqueous solution is about 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 through 90°C for a period of time which varies from about 30 seconds at 90°C to 30 minutes at 70°C.
8. A process as claimed in claim 6 in which the aqueous solution is maintained at an elevated temperature of from 75°C through 85°C for a period of time of from 5 through 3 minutes.
9. A process for lowering the gelling temperature of whey protein derived from milk which comprises forming an aqueous solution of whey proteins having a protein concentration of 3% weight/volume, adjusting the pH to about 8 with a dilute alkali metal hyroxide solution, raising the temperature of the solution to betwen 70°C and 90°C and maintaining the solution at the selected elevated temperature for a time varying from 30 minutes at 70°C to 30 seconds at 90°C, rapidly cooling the resultant modified solution to a temperature at which no further change in the protein occurs, adjusting the pH to from 6.5 through 7.0 and concentrating and drying to form a dry modified whey protein.
10. Whey protein having reduced gelling temperature whenever produced by the process of claim 1.
11. A process for lowering the gelling temperature of whey protein derived from milk which comprises subjecting whey to an ultra-filtration treatment, maintaining an aqueous solution of such whole whey proteins having a concentration of proteins of from 0.5 to 10% by weight/
volume at an elevated temperature of at least 70°C and at an alkaline pH to effect an increase in the sulphydryle groups available for reaction, the period of time over which the proteins are maintained at the elevated temper-ature and the pH of the solution both being selected such that precipitation, gelling and coagulation of the proteins while at the elevated temperatures is prevented, and cool-ing the resultant solution to a temperature at which no further change in the protein occurs.
volume at an elevated temperature of at least 70°C and at an alkaline pH to effect an increase in the sulphydryle groups available for reaction, the period of time over which the proteins are maintained at the elevated temper-ature and the pH of the solution both being selected such that precipitation, gelling and coagulation of the proteins while at the elevated temperatures is prevented, and cool-ing the resultant solution to a temperature at which no further change in the protein occurs.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB7923104 | 1979-07-03 | ||
| GB7923104A GB2055846B (en) | 1979-07-03 | 1979-07-03 | Process for lowering the gelling temperature of whey proteins obtained from milk |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1148536A true CA1148536A (en) | 1983-06-21 |
Family
ID=10506261
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000353770A Expired CA1148536A (en) | 1979-07-03 | 1980-06-11 | 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 |
| JP6995827B2 (en) | 2016-07-15 | 2022-01-17 | アーラ フーズ エエムビエ | Methods for Producing Concentrated or Dry Acid Gelable Whey Protein Aggregates and Related Compositions and Foods |
| 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 |
|---|---|
| NZ194216A (en) | 1982-05-25 |
| IE49694B1 (en) | 1985-11-27 |
| DK286380A (en) | 1981-01-04 |
| GB2055846A (en) | 1981-03-11 |
| JPH0150381B2 (en) | 1989-10-30 |
| GB2055846B (en) | 1983-02-23 |
| IT1145343B (en) | 1986-11-05 |
| FR2460630A1 (en) | 1981-01-30 |
| NL8003624A (en) | 1981-01-06 |
| IE801358L (en) | 1981-01-03 |
| AU532195B2 (en) | 1983-09-22 |
| IT8049069A0 (en) | 1980-06-25 |
| JPS5626159A (en) | 1981-03-13 |
| FR2460630B1 (en) | 1985-07-12 |
| DE3024356A1 (en) | 1981-01-22 |
| AU5942580A (en) | 1981-01-15 |
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| MKEX | Expiry |