Abstract
An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60 degrees C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus / classification
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Bacillus / enzymology*
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Enzyme Activation
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Enzyme Stability
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Hydrogen-Ion Concentration
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Industry
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Molecular Weight
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Serine Endopeptidases / analysis
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Serine Endopeptidases / chemistry*
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Serine Endopeptidases / isolation & purification*
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Species Specificity
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Temperature
Substances
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Serine Endopeptidases
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microbial serine proteinases