An extracellular endo-1,4-b-xylanase from Aspergillus japonicus: Purification, properties, and characterization of the encoding gene

An extracellular endo-1,4-b-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 sub(r) of 25.1 kDa. Xylanase ac...

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Published inJournal of bioscience and bioengineering Vol. 109; no. 3; pp. 227 - 229
Main Authors Wakiyama, Motoki, Yoshihara, Koji, Hayashi, Sachio, Ohta, Kazuyoshi
Format Journal Article
LanguageEnglish
Published 01.03.2010
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Summary:An extracellular endo-1,4-b-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 sub(r) of 25.1 kDa. Xylanase activity was optimal at pH 5.0 and 60 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.
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ISSN:1389-1723
DOI:10.1016/j.jbiosc.2009.09.005