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.
Publication types
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Comparative Study
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Evaluation Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus / classification
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Bacillus / enzymology*
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Bacillus / genetics*
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Bacillus subtilis / enzymology
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Bacillus subtilis / genetics
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Cloning, Molecular / methods
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Gene Expression Regulation, Bacterial / physiology
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Gene Expression Regulation, Enzymologic / physiology
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Molecular Sequence Data
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Molecular Weight
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Protein Engineering / methods*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics
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Sequence Homology, Amino Acid
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Serine Endopeptidases / biosynthesis*
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Serine Endopeptidases / chemistry*
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Serine Endopeptidases / classification
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Serine Endopeptidases / genetics
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Species Specificity
Substances
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Recombinant Proteins
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Serine Endopeptidases
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microbial serine proteinases