Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda.
dc.contributor.author | Rapp, P | |
dc.contributor.author | Wagner, F | |
dc.date.accessioned | 2015-07-30T12:13:03Z | en |
dc.date.available | 2015-07-30T12:13:03Z | en |
dc.date.issued | 1986-04 | en |
dc.identifier.citation | Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda. 1986, 51 (4):746-52 Appl. Environ. Microbiol. | en |
dc.identifier.issn | 0099-2240 | en |
dc.identifier.pmid | 16347038 | en |
dc.identifier.uri | http://hdl.handle.net/10033/561261 | en |
dc.description.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. | |
dc.language.iso | en | en |
dc.title | Production and Properties of Xylan-Degrading Enzymes from Cellulomonas uda. | en |
dc.type | Article | en |
dc.contributor.department | Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany. | en |
dc.identifier.journal | Applied and environmental microbiology | en |
refterms.dateFOA | 2018-06-13T05:27:33Z | |
html.description.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. |