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US4409248A Expired / Lapsed US ⏱️ 0.0 years remaining

Heat-gelling and foam-stabilizing enzymatically modified vegetable isolates

Assignee: Staley Continental Inc
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Filing: 1981-08-10
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Granted: 1983-10-11
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Expires: 2001-08-10
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Abstract

Abstract By enzymatically modifying vegetable glycoprotein isolates with an acid proteinase such as pepsin, the glycoproteins may be converted to a vegetable isolate useful as an egg albumin replacement or whip-stabilizing agent. The enzymatic modification partially hydrolyzes the glycoproteins and compositionally alters the glycoprotein subunit and aggregate structure. The enzymatic alteration produces a glycoprotein aggregate comprised of a plurality of subunits having saliently different physical and functional properties from that of the vegetable protein precursor source materials. The enzymatically modified vegetable isolates are capable of forming firm, white, opaque heat-set gels similar to those of egg albumin. The enzymatically modified glycoproteins are compatible with salt-containing recipes and functionally useful over a broad pH range.

Inventors

  • 👤 William F. Lehnhardt
  • 👤 Frank T. Orthoefer

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-11-06 03:06
CPC Classifications
A; A23; A23J; A23J1/00; A23J1/14; A23J3/00; A23J3/30; A23J3/32; A23J3/34; A23J3/346

Claims Analysis

Total Claims: 46
Claim 1
Independent Claim 163 words
An enzymatically modified vegetable protein composition possessing improved heat-gelling properties, prepared from 7S glycoproteins which contains (on a total protein weight basis), enzymatically modified 7S glycoprotein as the major protein component of the composition, said composition comprising enzymatically modified 7S protein in which the glycoprotein aggregates have an average molecular weight within the 200,000 to 300,000 molecular weight range, said glycoprotein aggregates consist essentially of a plurality of glycoprotein subunits of an average molecular weight of less than the glycoprotein subunit precursor source material for said enzymatically modified protein composition and the average electrophoretic migration value for the enzymatically modified subunits is less than that of the 7S glycoprotein subunits precursor source material for said composition, said composition being further characterized by forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 2
Dependent Claim 163 words
An enzymatically modified vegetable protein composition possessing improved heat-gelling properties, prepared from 7S glycoproteins which contains (on a total protein weight basis), enzymatically modified 7S glycoprotein as the major protein component of the composition, said composition comprising enzymatically modified 7S protein in which the glycoprotein aggregates have an average molecular weight within the 200,000 to 300,000 molecular weight range, said glycoprotein aggregates consist essentially of a plurality of glycoprotein subunits of an average molecular weight of less than the glycoprotein subunit precursor source material for said enzymatically modified protein composition and the average electrophoretic migration value for the enzymatically modified subunits is less than that of the 7S glycoprotein subunits precursor source material for said composition, said composition being further characterized by forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 3
Dependent Claim 19 words
The composition according to claim 1 wherein the glycoprotein source material consists essentially of 7S glycoproteins of soy proteins.
Claim 4
Dependent Claim 23 words
The composition according to claim 2 wherein the aggregate consists essentially of six glycoprotein subunits of an average molecular weight less than 48,000.
Claim 5
Dependent Claim 18 words
The composition according to claim 2 wherein the enzymatically modified composition comprises an acid proteinase modified 7S glycoprotein.
Claim 6
Dependent Claim 36 words
The composition according to claim 2 wherein the electrophoretic migrating value of the enzymatically modified subunit has a value of about 25% to about 50% of the migrating value for the α' and α precursor subunits.
Claim 7
Dependent Claim 36 words
The composition according to claim 3 wherein the aqueous solution thereof is characterized as heat-setting into a white, heat-set gel of a penetrometer value of less than 5 when heated at 85° C. for 15 minutes.
Claim 8
Dependent Claim 27 words
The composition according to claim 6 wherein the gel obtained from the glycoprotein aggregate composition is characterized as having a penetrometer value of less than 3 mm.
Claim 9
Dependent Claim 26 words
The composition according to claim 6 wherein the aqueous solution containing the glycoprotein aggregate composition is characterized as heat-setting into a heat-set gel within five minutes.
Claim 10
Dependent Claim 33 words
The composition according to claim 3 wherein the glycoprotein aggregate composition is characteized as having an average molecular weight of about 265,000 and the subunits have an average molecular weight of about 47,000.
Claim 11
Dependent Claim 47 words
The composition according to claim 9 wherein the composition consists essentially of pepsin modified glycoprotein aggregate and the electrophoretic migrating value for the pepsin modified subunits range from about 35% to 45% of the migrating value for the α' and α subunit precursor of said aggregate composition.
Claim 12
Dependent Claim 46 words
The composition according to claim 3 wherein the glycoprotein aggregate composition is characterized as having an average molecular weight within the 250,000 to 280,000 M.W. range, and heat-setting into a white, opaque, gel when the aqueous solution thereof is heated at 85° C. for 5 minutes.
Claim 13
Independent Claim 188 words
A method for providing a heat-gelling, enzymatically modified vegetable glycoprotein composition containing (on a weight basis) 7S glycoprotein as the major protein component of said composition, said method comprising enzymatically treating an aqueous vegetable solution which on a total protein weight basis contains 7S glycoprotein as the major vegetable protein component with proteinase to partially hydrolyze the glycoprotein into glycoprotein aggregates of an average molecular weight within the 200,000 to 300,000 molecular weight range in which the glycoprotein aggregates consisting essentially of a plurality of enzymatically modified glycoprotein subunits of an average molecular weight less than that of the unhydrolyzed glycoprotein subunit precursor source material for said enzymatically modified protein composition and, the enzymatically modified glycoprotein subunits are characterized as having an average electrophoretic migration value less than that of the unhydrolyzed subunits precursor source material for said composition, and said composition is being further characterized as forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 14
Independent Claim 188 words
A method for providing a heat-gelling, enzymatically modified vegetable glycoprotein composition containing (on a weight basis) 7S glycoprotein as the major protein component of said composition, said method comprising enzymatically treating an aqueous vegetable solution which on a total protein weight basis contains 7S glycoprotein as the major vegetable protein component with proteinase to partially hydrolyze the glycoprotein into glycoprotein aggregates of an average molecular weight within the 200,000 to 300,000 molecular weight range in which the glycoprotein aggregates consisting essentially of a plurality of enzymatically modified glycoprotein subunits of an average molecular weight less than that of the unhydrolyzed glycoprotein subunit precursor source material for said enzymatically modified protein composition and, the enzymatically modified glycoprotein subunits are characterized as having an average electrophoretic migration value less than that of the unhydrolyzed subunits precursor source material for said composition, and said composition is being further characterized as forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 15
Dependent Claim 15 words
The method according to claim 12 wherein the source material consists essentially of soy protein.
Claim 16
Dependent Claim 31 words
The method according to claim 12 wherein the soy protein comprises an enriched 7S fraction containing (on a weight basis) at least 70% by weight of the enzymatically modified 7S glycoprotein.
Claim 17
Dependent Claim 67 words
The method according to claim 14 wherein the 7S glycoprotein is hydrolyzed with an acid proteinase for a period of time sufficient and under hydrolyzing conditions to provide a glycoprotein aggregate of an average molecular weight within the 250,000 to 280,000 M.W. range and the glycoprotein aggregate consisting essentially of six subunits in which the subunit average molecular weight is greater than 40,000 but less than 50,000.
Claim 18
Dependent Claim 16 words
The method according to claim 15 wherein the 7S glycoprotein is hydrolyzed with an acid proteinase.
Claim 19
Dependent Claim 51 words
The method according to claim 14 wherein the 7S glycoprotein is hydrolyzed with an effective amount of a proteinase under conditions sufficient to provide a glycoprotein aggregate composition characterized as having an average molecular weight within the 250,000 to 280,000 range and the aggregate composition consists essentially of six glycoprotein subunits.
Claim 20
Dependent Claim 57 words
The method according to claim 17 wherein the hydrolysis of the 7S glycoprotein provides an aggregate composition which upon dissolution in water containing 0.1 M sodium chloride at pH 5.75 and 15% aggregate composition concentration (protein dry solids weight/water volume basis) and heating at 85° C. for 5 minutes will provide a white, solid, opaque heat-set gel.
Claim 21
Dependent Claim 41 words
The method according to claim 17 wherein the hydrolysis provides an aggregate composition characterized as having a migrating value ranging from about 25% to about 60% of the migrating value for the α' and α subunit precursors of said aggregate composition.
Claim 22
Dependent Claim 30 words
The method according to claim 17 wherein the aggregate composition is characterized as having an average molecular weight of about 265,000 and the average subunit molecular weight is about 47,000.
Claim 23
Dependent Claim 182 words
In a method for preparing a heat-set gel from an aqueous solution containing a protein as a heat-gelling agent, the improvement which comprises replacing at least a portion of the heat-gelling protein agent with an enzymatically modified vegetable protein composition comprised of enzymatically modified 7S glycoprotein aggregates as the major vegetable protein component (total vegetable protein weight basis) of said composition, said aggregates being characterized as having an average molecular weight within the 200,000 to 300,000 molecular weight range with the aggregates consisting essentially of a plurality of glycoprotein subunits of an average molecular weight less than the glycoprotein subunits precursor source material for said enzymatically modified glycoprotein composition and the enzymatically modified subunits have an average electrophoretic migration value less than that of the non-enzymatically modified subunit precursor source material for said composition, and said composition is further characterized as forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of solution is heated at 85° C. for 15 minutes.
Claim 24
Dependent Claim 182 words
In a method for preparing a heat-set gel from an aqueous solution containing a protein as a heat-gelling agent, the improvement which comprises replacing at least a portion of the heat-gelling protein agent with an enzymatically modified vegetable protein composition comprised of enzymatically modified 7S glycoprotein aggregates as the major vegetable protein component (total vegetable protein weight basis) of said composition, said aggregates being characterized as having an average molecular weight within the 200,000 to 300,000 molecular weight range with the aggregates consisting essentially of a plurality of glycoprotein subunits of an average molecular weight less than the glycoprotein subunits precursor source material for said enzymatically modified glycoprotein composition and the enzymatically modified subunits have an average electrophoretic migration value less than that of the non-enzymatically modified subunit precursor source material for said composition, and said composition is further characterized as forming a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said composition for each 100 ml of solution is heated at 85° C. for 15 minutes.
Claim 25
Dependent Claim 19 words
The method according to claim 21 wherein the enzymatically modified glycoprotein consists essentially of enzymatically modified 7S soy protein.
Claim 26
Dependent Claim 30 words
The method according to claim 22 wherein the composition is characterized as heat-setting within 5 minutes into a solid, opaque gel when the aqueous solution is heated at 85° C.
Claim 27
Dependent Claim 53 words
The method according to claim 22 wherein the aggregate composition is characterized as having an average molecular weight of about 250,000 to about 280,000 and the glycoprotein aggregate consists essentially of six subunits in which the average molecular weight for the individual subunits of said aggregate ranges from about 40,000 to 50,000 M.W.
Claim 28
Dependent Claim 34 words
The method according to claim 24 wherein the composition is characterized as forming a solid, white, heat-set gel of a penetrometer value less than 5 mm when heated at 85° C. for 15 minutes.
Claim 29
Dependent Claim 10 words
A heat-set gel containing the aggregate composition of claim 21.
Claim 30
Dependent Claim 10 words
A heat-set gel containing the aggregate composition of claim 22.
Claim 31
Dependent Claim 10 words
A heat-set gel containing the aggregate composition of claim 23.
Claim 32
Dependent Claim 10 words
A heat-set gel containing the aggregate composition of claim 24.
Claim 33
Dependent Claim 10 words
A heat-set gel containing the aggregate composition of claim 25.
Claim 34
Dependent Claim 195 words
In a method for preparing foamed product from an aqueous foaming composition containing a hydrophilic foaming agent wherein gas is ingested into the foaming composition to provide a foamed product, the improvement which comprises incorporating an effective amount of an enzymatically modified glycoprotein 7S aggregate composition into the foaming composition to stabilize the foamed product against degasification, said 7S glycoprotein aggregate composition being characterized as comprising an enriched 7S vegetable protein isolate wherein the 7S glycoprotein aggregates have an average molecular weight within the 200,000 to 300,000 molecular weight range, the aggregates of the enzymatically modified protein consisting essentially of a plurality of glycoprotein subunits of an average molecular weight less than that of the unmodified glycoprotein subunit source material for said enzymatically modified glycoprotein composition and the enzymatically modified subunits have an average electrophoretic migration value less than that of the unmodified glycoprotein subunits, and the aggregate composition is further characterized as providing a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said aggregrate composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 35
Dependent Claim 195 words
In a method for preparing foamed product from an aqueous foaming composition containing a hydrophilic foaming agent wherein gas is ingested into the foaming composition to provide a foamed product, the improvement which comprises incorporating an effective amount of an enzymatically modified glycoprotein 7S aggregate composition into the foaming composition to stabilize the foamed product against degasification, said 7S glycoprotein aggregate composition being characterized as comprising an enriched 7S vegetable protein isolate wherein the 7S glycoprotein aggregates have an average molecular weight within the 200,000 to 300,000 molecular weight range, the aggregates of the enzymatically modified protein consisting essentially of a plurality of glycoprotein subunits of an average molecular weight less than that of the unmodified glycoprotein subunit source material for said enzymatically modified glycoprotein composition and the enzymatically modified subunits have an average electrophoretic migration value less than that of the unmodified glycoprotein subunits, and the aggregate composition is further characterized as providing a solid, opaque gel when an aqueous solution adjusted to 0.1 M sodium chloride concentration and pH 5.75 and containing 15 protein grams of said aggregrate composition for each 100 ml of water is heated at 85° C. for 15 minutes.
Claim 36
Dependent Claim 19 words
The method according to claim 31 wherein the enzymatically modified glycoprotein consists essentially of enzymatically modified 7S soy protein.
Claim 37
Dependent Claim 28 words
The method according to claim 32 wherein at least a major weight portion of the hydrophilic foaming agent of said foaming composition comprises a vegetable protein whipping agent.
Claim 38
Dependent Claim 53 words
The method according to claim 32 wherein the aggregate composition is characterized as having an average molecular weight of about 250,000 to about 280,000 and the glycoprotein aggregate consists essentially of six subunits in which the average molecular weight for the individual subunits of said aggregate ranges from about 40,000 to 50,000 M.W.
Claim 39
Dependent Claim 53 words
The method according to claim 34 wherein the glycoprotein is enzymatically modified with an acid proteinase to provide an aggregate composition which upon dissolution in 100 ml water of 0.1 M sodium chloride concentration at pH 5.75 and heating at 85° C. for 5 minutes will provide a white, solid, opaque heat-set gel.
Claim 40
Dependent Claim 19 words
The method according to claim 34 wherein the hydrophilic foaming agent consists essentially of a vegetable protein whipping agent.
Claim 41
Dependent Claim 30 words
The method according to claim 32 wherein the aggregate composition is characterized as having an average molecular weight of about 265,000 and the average subunit molecular weight is about 47,000.
Claim 42
Dependent Claim 6 words
The foamed product of claim 32.
Claim 43
Dependent Claim 6 words
The foamed product of claim 33.
Claim 44
Dependent Claim 6 words
The foamed product of claim 35.
Claim 45
Dependent Claim 6 words
The foamed product of claim 36.
Claim 46
Dependent Claim 6 words
The foamed product of claim 37.

USPTO Annuity & Maintenance Windows

Annuity Stage Window Opens Payment Deadline Surcharge Period Until Estimated Fee Status
3.5 Years (Year 4) 1986-10-10 1987-04-11 1987-10-11 $2000.00 Window Closed / Lapsed
7.5 Years (Year 8) 1990-10-10 1991-04-11 1991-10-11 $3760.00 Window Closed / Lapsed
11.5 Years (Year 12) 1994-10-10 1995-04-11 1995-10-11 $7700.00 Window Closed / Lapsed

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