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Transglutaminase Catalyzed Cross‐Linking of Myosin to Soya Protein, Casein and Gluten
Author(s) -
KURTH L.,
ROGERS P. J.
Publication year - 1984
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.1365-2621.1984.tb12471.x
Subject(s) - tissue transglutaminase , gluten , casein , myosin , chemistry , biochemistry , food science , wheat gluten , enzyme
The covalent linkage of nonmeat proteins to myosin at temperatures and pH's common in meat product processing was investigated. Iodinated proteins were cross‐linked to immobilized myosin and then quantitated by gamma counting after noncross‐linked material was removed by washing with 6M guanidine hydrochloride. Bovine plasma transglutaminase catalyzed the formation of ε‐ (γ‐glutamyl) lysine cross‐links between myosin and soya protein, casein or gluten at 4‐5°C for 16 hr and at pH's from 5.5‐7.0. Casein was the best substrate with approximately 0.4g of casein cross‐linked to 1.0g myosin.