Xylan-hydrolysing enzymes of the yeast Pichia stipitis

Sabire Özcan, Peter Kötter, Michael Ciciary

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Two xylanolytic enzymes, xylanase and β-xylosidase from the yeast Pichia stipitis were purified to homogeneity and characterized. Both enzymes are secreted into the culture medium upon growth on xylan. The xylanase is a glycoprotein with an approximate molecular mass of 43 kDa. The N-linked carbohydrate content was estimated to be 26% by endoglycosidase H digestion. The β-xylosidase protein has a molecular mass of 37 kDa as determined by sodium dodecyl sulphate gel electrophoresis. Synthesis of xylanase was found to be inducible by xylan and repressible by xylose and glucose. By contrast, β-xylosidase is synthesized constitutively to a considerable degree. The purified β-xylosidase is able to hydrolyse aryl-β-D-glucosides with an even higher rate than β-xylosides. Thus, this enzyme may not be a specific component of the xylan-degrading system of P. stipitis.

Original languageEnglish
Pages (from-to)190-195
Number of pages6
JournalApplied Microbiology and Biotechnology
Issue number2
StatePublished - Nov 1991

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


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