Purification and substrate specificity of transglutaminases from blood andStreptoverticillium mobaraense

A procedure for a fast and simple purification of bovine plasma transglutam inase was developed, which resulted in a homogeneous enzyme preparation. Tw o different procedures were developed for the purification of pig erythrocy te transglutaminase, both of which resulted in partial purification. Both e nzymes were used in cross-linking reactions of alpha -lactalbumin, beta -la ctoglobulin, bovine serum albumin, casein, hemoglobin, glycinin, and myosin . The substrate specificity was compared to that of bacterial transglutamin ase isolated from Streptoverticillium mobaraense. The bacterial transglutam inase caused cross-linking of a wider range of proteins and, thus, exhibite d a lower substrate specificity than the blood transglutaminases. In additi on, differences exist in the necessity of the addition of reducing agents. These differences allow specific applications of blood and bacterial transg lutaminases at protein cross-linking in single or complex protein systems.