Journal
JOURNAL OF FOOD SCIENCE
Volume 66, Issue 1, Pages 25-29Publisher
INST FOOD TECHNOLOGISTS
DOI: 10.1111/j.1365-2621.2001.tb15576.x
Keywords
-
Categories
Ask authors/readers for more resources
A comparison was made of the deamidation activity of transglutaminases from 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available