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Appl Environ Microbiol. 1986 April; 51(4): 746-752
Copyright © 1986, American Society for Microbiology. All Rights Reserved.

Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda

¹ Gesellschaft für Biotechnologische Forschung mbH, and Institut für Biochemie und Biotechnologie der Universität Braunschweig, ² D-3300 Brunswick, Federal Republic of Germany

ABSTRACT

Xylan degradation and production of ß-xylanase and ß-xylosidase activities were studied in cultures of Cellulomonas uda grown on purified xylan from birchwood. ß-Xylanase activity was found to be associated with the cells, although in various degrees. The formation of ß-xylanase activity was induced by xylotriose and repressed by xylose. ß-Xylosidase activity was cell bound. Both constitutive and inducible ß-xylosidase activities were suggested. ß-Xylanase and ß-xylosidase activities were inhibited competitively by xylose. ß-Xylanase activity had a pronounced optimum pH of 5.8, whereas the optimum pH of ß-xylosidase activity ranged from 5.4 to 6.1. The major products of xylan degradation by a crude preparation of ß-xylanase activity, in decreasing order of amount, were xylobiose, xylotriose, xylose, and small amounts of xylotetraose. This pattern suggests that ß-xylanase activity secreted by C. uda is of the endosplitting type. Supernatants of cultures grown on cellulose showed not only ß-glucanase but also ß-xylanase activity. The latter could be attributed to an endo-1,4-ß-glucanase activity which had a low ß-xylanase activity.

^* Corresponding author.