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Purification and characterization of a xylanase fromBipolaris sorokiniana

Authors
Journal
Mycological Research
0953-7562
Publisher
Elsevier
Publication Date
Volume
98
Issue
1
Identifiers
DOI: 10.1016/s0953-7562(09)80339-0
Disciplines
  • Biology

Abstract

Bipolaris sorokiniana, a cereal fungal pathogen, showed xylanase activity when grown on minimal salt medium containing 2% of cell wall prepared from barley leaves as the sole carbon source. The most abundant of the xylanases, 1,4-β-D-xylan xylanohydrolase (EC 3.2.1.8), was purified to homogeneity by S-Sepharose chromatography, and its properties were determined. The induction of xylanase was highest on the 12th day after inoculation in shake flask culture. The purified xylanase had a molecular weight of 30 kDa and an isoelectric point of 9·5. The pH and temperature optima of the B. sorokiniana xylanase activity were 5·5 and 70°C respectively. The enzyme was stable over the pH range 5–10 but the stability towards temperature fell sharply above 55°.

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