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Updated: Aug 17, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Cloning and over-expression of an alkaline protease from Bacillus licheniformis
Xue-Ming Tang1, Wei Shen, F M Lakay
1The Key Laboratory of Industrial Biotechnology, Ministry of Education, Research Center of Industrial Microbiology, Southern Yangtze University, Wuxi 214036, P.R. China. txm@sun.ac.za
Abstract:
The alkaline protease gene, apr, from Bacillus licheniformis 2709 was cloned into a Bacillus shuttle expression vector, pHL, to yield the recombinant plasmid pHL-apr. The pHL-apr was expressed in Bacillus subtilis WB600, yielding a high expression strain BW-016. The amount of alkaline protease produced in the recombinant increased by 65% relative to the original strain. SDS-PAGE analysis indicated a Mr of 30.5 kDa. The amino acid sequence deduced from the DNA sequence analysis revealed a 98% identity to that of Bacillus licheniformis 6816.
