Deamidation of Several Food Proteins Using Free and Immobilized Ca^<2+>-Independent Microbial Transglutaminase

概要

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Enzymatic deamidation of α_<s1>-casein was done by using Ca^<2+>-independent microbial transglutaminase (MTGase) of a variant of Streptoverticillium mobaraense. Although the amount of deamidated glutamine residues in α_<s1>-casein was not as high as that of the case using guinea pig liver transglutaminase (GTGase), the improvements in pH-solubility and Ca^<2+>-sensitivity protile of the substrate protein were comparable to it. To do the enzymatic deamidation without chemical acylation of Lys residues of α_<s1>-casein, several immobilized MTGase were prepared with two types of chitosan beads. Although neither α^<s1>-casein nor β-casein was deamidated, dimethyl casein and citraconylated soy 7S globulin were deamidated by using the immobilized enzymes.
社団法人日本農芸化学会の論文
1996-03-23