Incorporation of Lysine- and Lysine Dipeptides into αs1-Casein by Ca2+-independent Microbial Transglutaminase

Abstract

Ca2 +-independent microbial transglutaminase of a variant of Streptoverticillium mobaraense was compared with Ca2+ -dependent guinea pig liver transglutaminase as a tool for incorporating lysine or lysine dipeptides into a food protein. The microbial enzyme was able to incorporate up to ca. 12 mol lysine into a mole of citra- conylated αsl-casein. Twenty two lysine dipeptides could be the substrate for incorporation catalyzed by the enzyme. The microbial enzyme showed much higher incorporation of lysine or lysine dipeptides than the guinea pig liver enzyme, which was attributed to the higher themostability of the microbial enzyme. © 1996, Taylor & Francis Group, LLC. All rights reserved.