| Literature DB >> 20159568 |
Motoki Wakiyama1, Koji Yoshihara, Sachio Hayashi, Kazuyoshi Ohta.
Abstract
An extracellular endo-1,4-beta-xylanase with specific activity of 566 U/mg was purified from the culture filtrate of a filamentous fungus, Aspergillus japonicus strain MU-2, grown on oat spelt xylan. The purified enzyme showed a single band on SDS-PAGE with an apparent M(r) of 25.1 kDa. Xylanase activity was optimal at pH 5.0 and 60 degrees C. The xylanase gene (xynA) encoded a 42 residue prepropeptide and a 191 residue mature protein. The XynA protein showed the highest sequence identity of 69% to Aspergillus niger XynB (DQ174549), which belongs to the glycoside hydrolase family 11. Copyright 2009 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.Entities:
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Year: 2009 PMID： 20159568 DOI： 10.1016/j.jbiosc.2009.09.005
Source DB: PubMed Journal: J Biosci Bioeng ISSN： 1347-4421 Impact factor: 2.894