No abstract

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-HPLCanalysis after enzymic digestion of the polymerized asl-casein showed existence of the £-(y-Glu)Lys bond. Thus, it was confirmed that the polymerization was formed by a catalytic reaction of the transglutaminase.

Several suspensions and emulsions containing commercial sodium caseinate or skim milk were gelatinized by Ca*+-independent microbial transglutaminase treatment. The characteristics of the gels were largely affected by the enzyme concentrations employed. For caseinate gels generally the higher enzyme concentration gave steep decreases in breaking strength, strain and cohesiveness of the gels. The creep tests on emulsified gels prepared to two different enzyme concentrations showed that the gel made with a higher enzyme concentration was the more viscoelastic. For skim milk gels, the enzyme treatment in higher concentration caused substantial increase of the breaking and hardness while the strain and cohesiveness had little or no changes.