Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor


Autoria(s): Carmona, E. C.; Brochetto-Braga, M. R.; Pizzirani-Kleiner, A. A.; Jorge, J. A.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

15/09/1998

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