Purification and characterization of a xylanase and an arabinofuranosidase from Bacillus polymyxa
Two hemicellulases from Bacillus polymyxa were purified and characterized: a xylanase with a molecular mass of 61 kD and pl of 4.7 and an arabinofuranosidase with a molecular mass of 166 kD and pl of 4.7. The xylanase, which showed increased thermostability in the presence of MgCl2, showed a typical endo-action mode on xylans from several sources. The arabinofuranosidase was only active on (1→5)-α-l-arabinooligosaccharides but not on linear (1→5)-α-l-arabinan, arabinogalactan, and arabinoxylan. However, it was able to release arabinose from arabinoxylan when an active endoxylanase was also present in hydrolysis assays
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| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | artículo biblioteca |
| Language: | English |
| Published: |
Elsevier
1995-05
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| Subjects: | Bacillus polymyxa, Xylanase, Arabinofuranosidase, Purification, |
| Online Access: | http://hdl.handle.net/10261/41913 http://dx.doi.org/10.13039/501100007273 |
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