Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58447
Type: Artigo de periódico
Title: PURIFICATION AND CHARACTERIZATION OF A NEW TRANSGLUTAMINASE FROM STREPTOMYCES SP ISOLATED IN BRAZILIAN SOIL
Author: Macedo, JA
Sette, LD
Sato, HH
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 45 kDa. 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 6.37 mM and a V(max) of 1.7 U/mL.
Country: EUA
Editor: Wiley-blackwell
Rights: fechado
Identifier DOI: 10.1111/j.1745-4514.2010.00456.x
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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