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Updated: May 29, 2026
Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
Efficient expression of an alkaline pectate lyase gene from Bacillus subtilis and the characterization of the
Yihan Liu1, Guanqun Chen, Jianling Wang
1Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin, 300457, People's Republic of China. lyh@tust.edu.cn
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.
