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Biopolymers Produced by Cross‐linking Soybean 11S Globulin with Whey Proteins using Transglutaminase
Author(s) -
YILDIRIM M.,
HETTIARACHCHY N.S.
Publication year - 1997
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1997.tb03983.x
Subject(s) - whey protein isolate , chemistry , whey protein , tissue transglutaminase , lactalbumin , differential scanning calorimetry , chromatography , globulin , biochemistry , legumin , high performance liquid chromatography , heterologous , storage protein , enzyme , biology , physics , gene , immunology , thermodynamics
Heterogeneity of biopolymers was determined by cross‐linking acetylated‐11S acidic subunits (Ac‐11S) of soy protein with α‐lactalbumin and β‐lactoglobulin. The extent of polymerization was determined by electrophoresis and HPLC. Differential scanning calorimetry (DSC) was used to determine thermal properties of starting proteins and biopolymers. HPLC data demonstrated the absence of biopolymers from Ac‐11S, acetylated α‐lactalbumin and acetylated β‐lactoglobulin when each was incubated separately with transglutaminase (TG). However, Ac‐11S formed biopolymers with α‐lactalbumin and β‐lactoglobulin when TG was added. TG catalyzed the formation of heterologous and homologous biopolymers from whey protein isolate (WPI) and soybean 11S globulin (11S). Cross‐linking WPI and 11S provided biopolymers with improved heat stability which may be useful to provide functionality to food products.