Purification and characterization of extracellular Staphylococcus warneri lipase
- 1 January 1995
- journal article
- research article
- Published by Springer Nature in Current Microbiology
- Vol. 30 (1) , 11-16
- https://doi.org/10.1007/bf00294517
Abstract
The extracellular lipase of Staphylococcus warneri was secreted as a protein with an apparent molecular mass of 90 kDa. It was then sequentially processed in the supernatant to a protein of 45 kDa. Tryptic digestion of the crude extract resulted in a homogeneous sample containing only the 45-kDa form. Purification was achieved by hydrophobic chromatography. Purified lipase had an optimum pH of 9.0 and an optimum temperature of 25°C. The enzyme was stable within the range pH 5.0–9.0; it had a broad substrate specificity. The results of inhibition studies were consistent with the view that lipases possess a serine residue at the catalytic site.Keywords
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