Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
15/09/1998
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Resumo |
An endoxylanase (beta-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a K-m of 6.5 mg ml(-1) and a V-max of 1440 U (mg protein)(-1). (C) 1998 Federation of European Microbiological Societies. Published by Elsevier B.V. B.V. All rights reserved. |
Formato |
311-315 |
Identificador |
http://dx.doi.org/10.1111/j.1574-6968.1998.tb13906.x Fems Microbiology Letters. Amsterdam: Elsevier B.V., v. 166, n. 2, p. 311-315, 1998. 0378-1097 http://hdl.handle.net/11449/31979 10.1111/j.1574-6968.1998.tb13906.x WOS:000076091500021 |
Idioma(s) |
eng |
Publicador |
Elsevier B.V. |
Relação |
FEMS Microbiology Letters |
Direitos |
closedAccess |
Palavras-Chave | #xylanase #endoxylanase #Aspergillus versicolor |
Tipo |
info:eu-repo/semantics/article |