Journal
JOURNAL OF MICROBIOLOGY
Volume 50, Issue 6, Pages 939-946Publisher
MICROBIOLOGICAL SOCIETY KOREA
DOI: 10.1007/s12275-012-2199-x
Keywords
serine protease; Verticillium lecanii; cloning; characterization
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Funding
- Ministry of Agriculture Key Projects of GM Cultivation of New Varieties, P. R. China [2009ZX08009-062B]
- Ministry of Agriculture Public Benefit and Industry Plan Project, P. R. China [201103016]
- International Cooperation Project in Changchun City [10GH26, 20100723]
- International Cooperation Project in Jilin Province [10GH26, 20100723]
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The entomopathogenic fungus Verticillium lecanii is a well-known biocontrol agent. V. lecanii produces subtilisin-like serine protease (Pr1), which is important in the biological control activity of some insect pests by degrading insect cuticles. In this study, a subtilisin-like serine protease gene VlPr1 was cloned from the fungus and the VlPr1 protein was expressed in Escherichia coli. The VlPr1 gene contains an open reading frame (ORF) interrupted by three short introns, and encodes a protein of 379 amino acids. Protein sequence analysis revealed high homology with subtilisin serine proteases. The molecular mass of the protease was 38 kDa, and the serine protease exhibited its maximal activity at 40A degrees C and pH 9.0. Protease activity was also affected by Mg2+ and Ca2+ concentration. The protease showed inhibitory activity against several plant pathogens, especially towards Fusarium moniliforme.
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