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PMID:8396026
| Citation |
Lesuisse, E, Schanck, K and Colson, C (1993) Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme. Eur. J. Biochem. 216:155-60 |
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| Abstract |
The extracellular lipase of Bacillus subtilis 168 was purified from the growth medium of an overproducing strain by ammonium sulfate precipitation followed by phenyl-Sepharose and hydroxyapatite column chromatography. The purified lipase had a strong tendency to aggregate. It exhibited a molecular mass of 19,000 Da by SDS-PAGE and a pI of 9.9 by chromatofocusing. The enzyme showed maximum stability at pH 12 and maximum activity at pH 10. The lipase was active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Using trioleyl glycerol as substrate, the enzyme preferentially cleaved the 1(3)-position ester bond. No interfacial activation effect was observed with triacetyl glycerol as substrate. |
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| Keywords |
Ammonium Sulfate; Bacillus subtilis/enzymology; Calcium/pharmacology; Chromatography, Thin Layer; Durapatite; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Hydrogen-Ion Concentration; Hydroxyapatites; Lipase/chemistry; Lipase/isolation & purification; Lipase/metabolism; Molecular Weight; Phenylmethylsulfonyl Fluoride/pharmacology; Substrate Specificity; Temperature; Triglycerides/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004806: triglyceride lipase activity |
ECO:0000314: |
F |
Table 2 shows esterase activity of estA lipase |
complete | ||||
|
enables |
GO:0004806: triglyceride lipase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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