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Purification and characterization of a GH11 xylanase from biobutanol-producing Clostridium beijerinckii G117.
- Source :
-
Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2015 Mar; Vol. 175 (6), pp. 2832-44. Date of Electronic Publication: 2015 Jan 07. - Publication Year :
- 2015
-
Abstract
- Most biobutanol-producing Clostridium strains are unable to ferment polysaccharides such as cellulose and xylan due to the lack of hydrolyzing enzymes. In this study, we show that Clostridium beijerinckii G117, a newly isolated biobutanol-producing strain, expresses xylanase enzyme in the presence of 1% beechwood xylan. The xylanase activity in the medium containing actively growing culture and 1% of beechwood xylan can reach up to 2.66 U/ml after 14 h of fermentation. Using salting-out and size-exclusion chromatography, we purify the crude xylanase by 8.7-fold from the supernatant with a yield of 32.2%. This purified xylanase has a molecular weight of 22.6 kDa, making it one of the smallest reported clostridial xylanases. Conserved domain analysis reveals that the xylanase belongs to glycoside hydrolase family 11 (GH11) but lacks a carbohydrate binding domain. When beechwood xylan is used as substrate for the xylanase, majority of the products are xylo-oligosaccharide (~98%), suggesting that this is an endo-1,4-β-xylanase.
- Subjects :
- Clostridium beijerinckii chemistry
Clostridium beijerinckii genetics
Clostridium beijerinckii metabolism
Endo-1,4-beta Xylanases genetics
Endo-1,4-beta Xylanases metabolism
Molecular Weight
Protein Structure, Tertiary
Xylans metabolism
Butanols metabolism
Clostridium beijerinckii enzymology
Endo-1,4-beta Xylanases chemistry
Endo-1,4-beta Xylanases isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 1559-0291
- Volume :
- 175
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Applied biochemistry and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 25564206
- Full Text :
- https://doi.org/10.1007/s12010-014-1470-5