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Comparison of Deamidation Activity of Transglutaminases
Author(s) -
Ohtsuka T.,
Umezawa Y.,
Nio N.,
Kubota K.
Publication year - 2001
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.1365-2621.2001.tb15576.x
Subject(s) - deamidation , chemistry , biochemistry , casein , guinea pig , substrate (aquarium) , glutamine , amino acid , enzyme , biology , ecology , endocrinology
A comparison was made of the deamidation activity of transglutaminases fro m guinea pig liver (GTGase), fish red sea bream liver (FTGase) and microorganisms (MTGase). Against the Z‐Gln‐Gly, kinetic constants of the deamidation and incorporation of primary amine were measured. GTGase and FTGase showed similar deamidation activity, however, that of MTGase was less than 1/7 of the other two TGases. Against the proteins, N, N‐dimethylated casein and native gliadin, FTGase was the most active and deamidated respectively 45.5% and 38.2% of Gln residues. The deamidation rate of these proteins by GTGase was less than 1/2 and these results were expected to be caused by the difference of substrate specificity of the TGases.