Polymerization of several proteins by Ca2+-independent transglutaminase derived from microorganisms.

Abstract

αs1-Casein and soybean globulins were polymerized and gelatinized by Ca2+-independent transglutaminase that was isolated from the culture filtrate of a microorganism thought to belong to Streptoverticillium sp. of actinomycetes. This enzyme polymerized such albumins as bovine serum albumin, human serum albumin and conalbumin in the presence of dithiothreitol. Rabbit myosin was polymerized by the present emzyme but actin was not. An RP-HPLC analysis after enzymic digestion of the polymerized αs1-casein showed existence of the ε-(γ-Glu)Lys bond. Thus, it was confirmed that the polymerization was formed by a catalytic reaction of the transglutaminase.