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|Title:||Production, Purification, and Characterization of a Xylooligosaccharides-forming Xylanase from High-butanol-producing Strain Clostridium sp. BOH3||Authors:||Rajagopalan, G.
|Issue Date:||Jun-2013||Citation:||Rajagopalan, G., Yew, K.W., He, J., Yang, K.L. (2013-06). Production, Purification, and Characterization of a Xylooligosaccharides-forming Xylanase from High-butanol-producing Strain Clostridium sp. BOH3. Bioenergy Research 6 (2) : 448-457. ScholarBank@NUS Repository. https://doi.org/10.1007/s12155-012-9259-2||Abstract:||An endo-acting xylanase is isolated from the culture medium of Clostridium sp. BOH3 when xylan, glucose, xylose, or sugarcane bagasse hydrolysate (SBH) is used as a carbon source. Crude xylanase is purified by using an anionic Q-column with a yield of 39 %. The pure xylanase has a molecular weight of 35. 8 kDa, and it shows optimal activity at pH 5 and 60 °C. When beechwood xylan is used as a substrate, this xylanase liberates short oligosaccharides (XOS) predominantly, ranging from xylobiose (X2) to xylopentaose (X5). However, no xylose can be detected, suggesting that this is an endo-β-1,4-xylanase. Kinetic study of this xylanase reveals that Km and Vmax are 1. 36 mg/ml and 212 μmol/(min. mg protein), respectively. On the basis of amino acid sequence, this enzyme shows homology to xylanase (xynb) from Clostridium acetobutylicum ATCC 824, but this enzyme has several distinctive characteristics. For example, its activity can be enhanced with the addition of divalent metal ions, and it produces XOS exclusively when xylan is used as a substrate. These unique characteristics suggest that this is a new enzyme. © 2012 Springer Science+Business Media New York.||Source Title:||Bioenergy Research||URI:||http://scholarbank.nus.edu.sg/handle/10635/89944||ISSN:||19391234||DOI:||10.1007/s12155-012-9259-2|
|Appears in Collections:||Staff Publications|
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