Efficient expression of an alkaline pectate lyase gene from Bacillus subtilis and the characterization of the recombinant protein |
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| Authors: | Yihan Liu Guanqun Chen Jianling Wang Yujie Hao Ming Li Yu Li Bo Hu Fuping Lu |
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| Institution: | (1) Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin, 300457, People’s Republic of China;(2) Department of Agricultural, Food & Nutritional Science, University of Alberta, Edmonton, AB, T6G 2P5, Canada;(3) National Engineering Laboratory for Industrial Enzymes, Tianjin, 300457, People’s Republic of China;(4) Tianjin Key Laboratory of Industrial Microbiology, Tianjin, 300457, People’s Republic of China;(5) College of Biotechnology, Tianjin University of Science and Technology, Tianjin, 300457, People’s Republic of China |
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| 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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