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An alkali-tolerant xylanase produced by the newly isolated alkaliphilic Bacillus pumilus from paper mill effluent.

Authors
  • Wang, Jing
  • Zhang, Wei-wei
  • Liu, Jin-ni
  • Cao, Yao-ling
  • Bai, Xiao-ting
  • Gong, Yue-sheng
  • Cen, Pei-lin
  • Yang, Ming-ming
Type
Published Article
Journal
Molecular Biology Reports
Publisher
Springer-Verlag
Publication Date
Oct 01, 2010
Volume
37
Issue
7
Pages
3297–3302
Identifiers
DOI: 10.1007/s11033-009-9915-6
PMID: 19949874
Source
Medline
License
Unknown

Abstract

An alkaline active xylanase, XynBYG, was purified from an alkaliphilic Bacillus pumilus BYG, which was newly isolated from paper mill effluent. It had an optimum pH of 8.0-9.0, and showed good stability after incubated at pH 9.0 for 120 min. The optimum temperature for the activity was 50°C, and the enzyme retained below 55% of its original activity for 30 min at 55°C. The gene coding for XynBYG consists of 687 bp and encodes 229 amino acids. Similarity analysis indicated that XynBYG belong to family 11 glycosyl hydrolases. Site-directed mutagenesis was performed to replace five sites (Tyr/Ser) to Arg/Glu and the results demonstrated that the optimum temperature of the mutant Y7 (S39R-T146E) increased 5°C and the half-life of inactivation (T1/2) at 60 and 65°C was 1 h and 25 min, respectively. Thus, it provides a potential xylanase that can meet the harsh conditions in the industrial applications.

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