2.50
Hdl Handle:
http://hdl.handle.net/10033/561261
Title:
Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda.
Authors:
Rapp, P; Wagner, F
Abstract:
Xylan degradation and production of beta-xylanase and beta-xylosidase activities were studied in cultures of Cellulomonas uda grown on purified xylan from birchwood. beta-Xylanase activity was found to be associated with the cells, although in various degrees. The formation of beta-xylanase activity was induced by xylotriose and repressed by xylose. beta-Xylosidase activity was cell bound. Both constitutive and inducible beta-xylosidase activities were suggested. beta-Xylanase and beta-xylosidase activities were inhibited competitively by xylose. beta-Xylanase activity had a pronounced optimum pH of 5.8, whereas the optimum pH of beta-xylosidase activity ranged from 5.4 to 6.1. The major products of xylan degradation by a crude preparation of beta-xylanase activity, in decreasing order of amount, were xylobiose, xylotriose, xylose, and small amounts of xylotetraose. This pattern suggests that beta-xylanase activity secreted by C. uda is of the endosplitting type. Supernatants of cultures grown on cellulose showed not only beta-glucanase but also beta-xylanase activity. The latter could be attributed to an endo-1,4-beta-glucanase activity which had a low beta-xylanase activity.
Affiliation:
Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.
Citation:
Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda. 1986, 51 (4):746-52 Appl. Environ. Microbiol.
Journal:
Applied and environmental microbiology
Issue Date:
Apr-1986
URI:
http://hdl.handle.net/10033/561261
PubMed ID:
16347038
Type:
Article
Language:
en
ISSN:
0099-2240
Appears in Collections:
Publications of Division of Biochemical Engineering (BVT)

Full metadata record

DC FieldValue Language
dc.contributor.authorRapp, Pen
dc.contributor.authorWagner, Fen
dc.date.accessioned2015-07-30T12:13:03Zen
dc.date.available2015-07-30T12:13:03Zen
dc.date.issued1986-04en
dc.identifier.citationProduction and Properties of Xylan-Degrading Enzymes from Cellulomonas uda. 1986, 51 (4):746-52 Appl. Environ. Microbiol.en
dc.identifier.issn0099-2240en
dc.identifier.pmid16347038en
dc.identifier.urihttp://hdl.handle.net/10033/561261en
dc.description.abstractXylan degradation and production of beta-xylanase and beta-xylosidase activities were studied in cultures of Cellulomonas uda grown on purified xylan from birchwood. beta-Xylanase activity was found to be associated with the cells, although in various degrees. The formation of beta-xylanase activity was induced by xylotriose and repressed by xylose. beta-Xylosidase activity was cell bound. Both constitutive and inducible beta-xylosidase activities were suggested. beta-Xylanase and beta-xylosidase activities were inhibited competitively by xylose. beta-Xylanase activity had a pronounced optimum pH of 5.8, whereas the optimum pH of beta-xylosidase activity ranged from 5.4 to 6.1. The major products of xylan degradation by a crude preparation of beta-xylanase activity, in decreasing order of amount, were xylobiose, xylotriose, xylose, and small amounts of xylotetraose. This pattern suggests that beta-xylanase activity secreted by C. uda is of the endosplitting type. Supernatants of cultures grown on cellulose showed not only beta-glucanase but also beta-xylanase activity. The latter could be attributed to an endo-1,4-beta-glucanase activity which had a low beta-xylanase activity.en
dc.language.isoenen
dc.titleProduction and Properties of Xylan-Degrading Enzymes from Cellulomonas uda.en
dc.typeArticleen
dc.contributor.departmentGesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.en
dc.identifier.journalApplied and environmental microbiologyen
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