Purification and characterization of a GH11 xylanase from biobutanol-producing Clostridium beijerinckii G117.
Appl Biochem Biotechnol
; 175(6): 2832-44, 2015 Mar.
Article
em En
| MEDLINE
| ID: mdl-25564206
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-ß-xylanase.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endo-1,4-beta-Xilanases
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Clostridium beijerinckii
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Butanóis
Idioma:
En
Revista:
Appl Biochem Biotechnol
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Singapura
País de publicação:
EEUU
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ESTADOS UNIDOS
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ESTADOS UNIDOS DA AMERICA
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EUA
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UNITED STATES
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UNITED STATES OF AMERICA
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US
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USA