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Directed evolution of xylanase J from alkaliphilic Bacillus sp. strain 41M-1: restore of alkaliphily of a mutant with an acidic pH optimum
Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177QΔJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177QΔJC and G32...
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Published in: | Nucleic Acids Symposium Series 2003-09, Vol.3 (1), p.315-316 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Citations: | Items that cite this one |
Online Access: | Request full text |
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Summary: | Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177QΔJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177QΔJC and G32V/Y176D/E177QΔJC, retained about 30% and 43% activity of their maximal activities and 43% activity of their maximal activities at pH 6.0, respectively. |
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ISSN: | 0261-3166 1746-8272 |
DOI: | 10.1093/nass/3.1.315 |