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Gel Point of Whey and Egg Proteins Using Dynamic Rheological Data
Author(s) -
HSIEH YIN LIANG,
REGENSTEIN JOE M.,
RAO M. ANANDHA
Publication year - 1993
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.1365-2621.1993.tb03223.x
Subject(s) - ovotransferrin , egg white , ovalbumin , whey protein , chemistry , whey protein isolate , rheology , disulfide bond , chromatography , beta lactoglobulin , food science , biochemistry , materials science , biology , immune system , immunology , composite material
The gel point temperatures of coagulation type proteins and gelation type proteins were determined by extrapolating the rapidly rising phase of the storage modulus G’back to the temperature axis. The gelation onset. temperatures of the concentration‐independent proteins oval‐bumin, ovotransferrin, and BSA were 81°C, 62°C, and 75°, respectively, Gelation of whey protein isolate and egg white gels, both concentration‐dependent, was presumably due to disulfide bonds formed by the interactions of the concentration‐independent proteins: α‐lac‐talbumin and β‐lactoglobulin, and ovalbumin and ovotransferrin, respectively. Moreover, the incipient gel temperature of whey proteins decreased when the concentration of whey proteins increased.