Abstract
A preparative method for purification of a novel protease from the psychrotolerant Gram-negative microorganism Serratia proteamaculans (PSP) was developed using affinity chromatography on BPTI-Sepharose. It yielded electrophoretically homogeneous PSP preparation of 60 kD. The PSP properties (temperature and pH stability, high catalytic efficiency) indicate that this enzyme can be defined as a psychrophilic protease. Inhibitory analysis together with substrate specificity indicates that the studied PSP exhibits properties of serine trypsin-like and Zn-dependent protease.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / antagonists & inhibitors
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism
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Chromatography, Affinity / methods
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Chromatography, Ion Exchange / methods
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Enzyme Stability / drug effects
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Hydrogen-Ion Concentration
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Kinetics
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Peptide Hydrolases / isolation & purification
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Peptide Hydrolases / metabolism*
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Protease Inhibitors / pharmacology
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Serratia / enzymology*
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Substrate Specificity
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Temperature
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Trypsin / metabolism*
Substances
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Bacterial Proteins
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Protease Inhibitors
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Peptide Hydrolases
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Trypsin