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Construction, Expression, and Characterization of a Thermostable Xylanase

Construction, Expression, and Characterization of a Thermostable Xylanase A hybrid gene, btx, encoding a thermostable xylanase, Btx, was constructed by substituting the 31 N-terminal amino acid residues of the Thermomonospora fusca xylanase A (TfxA) for the corresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A (BsxA). The btx gene was expressed in Escherichia coli BL21. The halo size produced by xylanase Btx on a Remanzol brilliant blue R (RBB) xylan plate at 60°C and pH 6.0 was larger than those of BsxA and TfxA. The molecular weight of Btx was 22 kDa. Temperature and pH optima for Btx were at 50–60°C and 6.0, respectively. Btx showed activity over 80% over a pH range of 5.0–9.0, which was wider than that of BsxA, and was also more acid-resistant than TfxA. Btx exhibited significant thermostability compared with BsxA. The results show the importance of the N-terminal sequence of TfxA in thermostability. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Microbiology Springer Journals

Construction, Expression, and Characterization of a Thermostable Xylanase

Current Microbiology , Volume 51 (3) – Aug 2, 2005

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References (20)

Publisher
Springer Journals
Copyright
Copyright © 2005 by Springer Science+Business Media, Inc.
Subject
Life Sciences; Biotechnology; Microbiology
ISSN
0343-8651
eISSN
1432-0991
DOI
10.1007/s00284-005-4543-4
pmid
16086105
Publisher site
See Article on Publisher Site

Abstract

A hybrid gene, btx, encoding a thermostable xylanase, Btx, was constructed by substituting the 31 N-terminal amino acid residues of the Thermomonospora fusca xylanase A (TfxA) for the corresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A (BsxA). The btx gene was expressed in Escherichia coli BL21. The halo size produced by xylanase Btx on a Remanzol brilliant blue R (RBB) xylan plate at 60°C and pH 6.0 was larger than those of BsxA and TfxA. The molecular weight of Btx was 22 kDa. Temperature and pH optima for Btx were at 50–60°C and 6.0, respectively. Btx showed activity over 80% over a pH range of 5.0–9.0, which was wider than that of BsxA, and was also more acid-resistant than TfxA. Btx exhibited significant thermostability compared with BsxA. The results show the importance of the N-terminal sequence of TfxA in thermostability.

Journal

Current MicrobiologySpringer Journals

Published: Aug 2, 2005

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