Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense
article
A procedure for a fast and simple purification of bovine plasma transglutaminase was developed, which resulted in a homogeneous enzyme preparation. Two different procedures were developed for the purification of pig erythrocyte transglutaminase, both of which resulted in partial purification. Both enzymes were used in cross-linking reactions of α-lactalbumin, β-lactoglobulin, bovine serum albumin, casein, hemoglobin, glycinin, and myosin. The substrate specificity was compared to that of bacterial transglutaminase isolated from Streptoverticillium mobaraense. The bacterial transglutaminase caused cross-linking of a wider range of proteins and, thus, exhibited a lower substrate specificity than the blood transglutaminases. In addition, differences exist in the necessity of the addition of reducing agents. These differences allow specific applications of blood and bacterial transglutaminases at protein cross-linking in single or complex protein systems. Chemicals/CAS: Transglutaminases, EC 2.3.2.13
Topics
TNO Identifier
41994
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 49(7), pp. 3389-3393.
Pages
3389-3393
Files
To receive the publication files, please send an e-mail request to TNO Repository.