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DC Field | Value | Language |
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dc.contributor.author | Shrinivas, D | |
dc.contributor.author | Savitha, G | |
dc.contributor.author | Raviranjan, K | |
dc.contributor.author | Naik, GR | |
dc.date.accessioned | 2020-06-12T15:04:11Z | - |
dc.date.available | 2020-06-12T15:04:11Z | - |
dc.date.issued | 2010 | |
dc.identifier.citation | APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY , Vol. 162 , 7 , p. 2049 - 2057 | en_US |
dc.identifier.uri | 10.1007/s12010-010-8980-6 | |
dc.identifier.uri | http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4547 | - |
dc.description.abstract | A highly thermostable alkaline xylanase was purified to homogeneity from culture supernatant of Bacillus sp. JB 99 using DEAE-Sepharose and Sephadex G-100 gel filtration with 25.7-fold increase in activity and 43.5% recovery. The molecular weight of the purified xylanase was found to be 20 kDA by SDS-PAGE and zymogram analysis. The enzyme was optimally active at 70 A degrees C, pH 8.0 and stable over pH range of 6.0-10.0.The relative activity at 9.0 and 10.0 were 90% and 85% of that of pH 8.0, respectively. The enzyme showed high thermal stability at 60 A degrees C with 95% of its activity after 5 h. The K (m) and V (max) of enzyme for oat spelt xylan were 4.8 mg/ml and 218.6 A mu M min(-1) mg(-1), respectively. Analysis of N-terminal amino acid sequence revealed that the xylanase belongs to glycosyl hydrolase family 11 from thermoalkalophilic Bacillus sp. with basic pI. Substrate specificity showed a high activity on xylan-containing substrate and cellulase-free nature. The hydrolyzed product pattern of oat spelt xylan on thin-layer chromatography suggested xylanase as an endoxylanase. Due to these properties, xylanase from Bacillus sp. JB 99 was found to be highly compatible for paper and pulp industry. | en_US |
dc.publisher | SPRINGER | |
dc.subject | Bacillus sp JB 99 | |
dc.subject | Thermoalkalophilic | |
dc.subject | Xylanase | |
dc.subject | Purification | |
dc.subject | Glycosyl hydrolases | |
dc.title | A Highly Thermostable Alkaline Cellulase-Free Xylanase from Thermoalkalophilic Bacillus sp JB 99 Suitable for Paper and Pulp Industry: Purification and Characterization | en_US |
dc.type | Article | |
Appears in Collections: | 1. Journal Articles |
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