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A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization

Paper ID Volume ID Publish Year Pages File Format Full-Text
18474 42724 2006 7 PDF Available
Title
A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization
Abstract

A thermostable, alkaline active xylanase was purified to homogeneity from the culture supernatant of an alkaliphilic Bacillus halodurans S7, which was isolated from a soda lake in the Ethiopian Rift Valley. The molecular weight and the pI of this enzyme were estimated to be around 43 kDa and 4.5, respectively. When assayed at 70 °C, it was optimally active at pH 9.0–9.5. The optimum temperature for the activity was 75 °C at pH 9 and 70 °C at pH 10. The enzyme was stable over a broad pH range and showed good thermal stability when incubated at 65 °C in pH 9 buffer. The enzyme activity was strongly inhibited by Mn2+. Partial inhibition was also observed in the presence of 5 mM Cu2+, Co2+ and EDTA. Inhibition by Hg2+ and dithiothreitol was insignificant. The enzyme was free from cellulase activity and degraded xylan in an endo-fashion.

Keywords
Xylanase; Alkaliphile; Bacillus
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A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 7, 3 November 2006, Pages 1492–1498
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us