Print Email Facebook Twitter Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense 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 18.104.22.168 Subject NutritionAnimalsCattleCross ReactionsErythrocytesStreptomycetaceaeSubstrate SpecificitySwineTransglutaminasesAnimaliaBacteria (microorganisms)Bos taurusBovinaeStreptomycesStreptomyces mobaraensisSus scrofa To reference this document use: 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 Files To receive the publication files, please send an e-mail request to TNO Library.