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Efficient expression of an alkaline pectate lyase gene from Bacillus subtilis and the characterization of the recombinant protein.

Authors
  • Liu, Yihan
  • Chen, Guanqun
  • Wang, Jianling
  • Hao, Yujie
  • Li, Ming
  • Li, Yu
  • Hu, Bo
  • Lu, Fuping
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Jan 01, 2012
Volume
34
Issue
1
Pages
109–115
Identifiers
DOI: 10.1007/s10529-011-0734-1
PMID: 21915717
Source
Medline
License
Unknown

Abstract

The gene encoding a novel alkaline pectate lyase (Apel) from Bacillus subtilis was cloned and expressed in B. subtilis WB600. Apel contained an ORF of 1,260 bp, encoding a signal peptide of 21 amino acids and a mature protein of 399 amino acids with a calculated molecular mass of 45497.9 Da. The mature Apel was structurally related to the enzymes in the polysaccharide lyase family 1. After purification, the recombinant Apel had a specific activity of 445 U mg(-1). The enzyme was optimally active at 50°C and pH 9.

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