Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/108679
Type: Artigo de periódico
Title: Purification And Characterization Of A New Transglutaminase From Streptomyces Sp. Isolated In Brazilian Soil
Author: Macedo J.A.
Sette L.D.
Sato H.H.
Abstract: A new microbial transglutaminase (MTGase or MTG, EC 2.3.2.13) from a Streptomyces sp. strain isolated from Brazilian soil samples was purified and characterized. Enzyme purification was fast and simple, consisting of two successive chromatographies on Sephadex G-75 columns with yields of 48 and 17%, respectively. The protein purification was successfully achieved to electrophoretical homogeneity on sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The molecular mass of the MTGase was estimated to be about 45kDa. The enzyme exhibited optimal activity in the pH range of 6.0-6.5 and at 35-40C. It was stable over a broad pH range (4.5-8.0) and up to 45C. The purified MTG's activity was independent of Ca +2, but was activated by the presence of K +, Ba 2+, Na +, and Co 2+, and inhibited by Cu 2+ and Hg 2+, which suggests a thiol group at its active site. The purified enzyme presented a K m of 6.37mM and a V max of 1.7U/mL. © 2011 Wiley Periodicals, Inc..
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Rights: fechado
Identifier DOI: 10.1111/j.1745-4514.2010.00456.x
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-79960951240&partnerID=40&md5=74b986477f24a44d75322387c14d7c4a
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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