Title
Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense
Author
de Jong, G.A.H.
Wijngaards, G.
Boumans, H.
Koppelman, S.
Hessing, M.
Centraal Instituut voor Voedingsonderzoek TNO
Publication year
2001
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
Subject
Nutrition
Animals
Cattle
Cross Reactions
Erythrocytes
Streptomycetaceae
Substrate Specificity
Swine
Transglutaminases
Animalia
Bacteria (microorganisms)
Bos taurus
Bovinae
Streptomyces
Streptomyces mobaraensis
Sus scrofa
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http://resolver.tudelft.nl/uuid:fe3d11d0-3d2f-47f3-8d47-9dd6a632594d
DOI
https://doi.org/10.1021/jf001162h
TNO identifier
41994
ISSN
0021-8561
Source
Journal of Agricultural and Food Chemistry, 49 (7), 3389-3393
Document type
article