Purification, characterization and amplification of a 1.8 kbp fragment of xylanase 5 from <i>Aeromonas caviae </i>W-61
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Title |
Purification, characterization and amplification of a 1.8 kbp fragment of xylanase 5 from Aeromonas caviae W-61
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Creator |
Roy, Narayan
Kamio, Yoshiyuki |
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Description |
179-184
Aeromonas caviae W-61 produces multiple extracellular xylanases, the xylanases 1,2,3,4, and 5. In this study, we purified and characterized the xylanase 5 of A. caviae W-61, and amplified a part of xylanase 5 gene (xyn5). The purified xylanase 5 was found to be a single polypeptide with molecular mass of 140 kDa. It was an endo-β-1 ,4-xylanase showing optimum temperature 40oC and optimum pH 6.0. Xylobiose, xylotriose, xylotetrose, xylopentose, xylohexose and a small amount of xylose were detected as the hydrolysis products. The N-terminal amino acid sequence and several internal amino acid sequences of xylanases 5 were determined. From the sequence, a 1.8 kbp fragment was amplified by PCR using forward and reverse primers. DNA sequencing confirmed the presence of nucleotide sequences corresponding to the N-terminal amino acid sequence and the internal amino acid sequences of xylanase 5. |
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Date |
2013-07-15T08:51:39Z
2013-07-15T08:51:39Z 2002-06 |
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Type |
Article
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Identifier |
0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19775 |
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Language |
en_US
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Rights |
CC Attribution-Noncommercial-No Derivative Works 2.5 India
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Publisher |
NISCAIR-CSIR, India
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Source |
IJBB Vol.39(3) [June 2002]
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