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Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense

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Author: Jong, G.A.H. de · Wijngaards, G. · Boumans, H. · Koppelman, S. · Hessing, M.
Type:article
Date:2001
Institution: Centraal Instituut voor Voedingsonderzoek TNO
Source:Journal of Agricultural and Food Chemistry, 7, 49, 3389-3393
Identifier: 41994
doi: doi:10.1021/jf001162h
Keywords: Nutrition · Animals · Cattle · Cross Reactions · Erythrocytes · Streptomycetaceae · Substrate Specificity · Swine · Transglutaminases · Animalia · Bacteria (microorganisms) · Bos taurus · Bovinae · Streptomyces · Streptomyces mobaraensis · Sus scrofa

Abstract

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