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Xylan-hydrolysing enzymes of the yeastPichia stipitis

✍ Scribed by Sabire Özcan; Peter Kötter; Michael Ciciary

Publisher
Springer
Year
1991
Tongue
English
Weight
796 KB
Volume
36
Category
Article
ISSN
1432-0614

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✦ Synopsis

Two xylanolytic enzymes, xylanase and flxylosidase 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 fl-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, fl-xylosidase is synthesized constitutively to a considerable degree. The purified fl-xylosidase is able to hydrolyse aryl-fl-D-glucosides with an even higher rate than fl-xylosides. Thus, this enzyme may not be a specific component of the xylan-degrading system of P. stipitis.

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