Purification and characterization of a xylanase from Bipolaris sorokiniana

Sari Peltonen, Reijo Karjalainen, Marja-Leena Niku-Paavola

Research output: Contribution to journalArticleScientificpeer-review

11 Citations (Scopus)


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, 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°.
Original languageEnglish
Pages (from-to)67-73
JournalMycological Research
Issue number1
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed


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