Studies on xylanase system of thermophilic fungi. III. Enzymatic properties of .BETA.-xylosidase from Malbranchea pulchella var. sulfurea No. 48.
- 1 January 1977
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (9) , 1601-1606
- https://doi.org/10.1271/bbb1961.41.1601
Abstract
Some enzymatic properties of Malbranchea β-xylosidase were investigated. The β-xylosidase activity was inhibited by Hg2+, Zn2+, Cu2+, N-bromosuccinimide, p-chloromercuri-benzoate and sodium laurylsulfate, while this activity was activated by Ca2+. The enzyme released xylose as the end product even from 10% xylobiose solution without forming any xylooligosaccharides. The enzyme well acted on aryl-β-D-xylosides, but showed no activity on alkyl-β-D-xylosides, and it was practically free from glucosidase activity. The Km and Vmax, values of this enzyme for xylobiose were calculated to be 2.86×10-3M and 34.5 μmoles/mg/min, respectively, and these values determined for phenyl-β-D-xyloside were 3.01×10-3M and 16.2 μmoles/mg/min, respectively.Keywords
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