Isolation and characterization of a staphylococcal lipase.
A number of coagulase-negative staphylococci isolated from human skin were found to produce lipase. Lipolytic activity appeared in the growth medium during the stationary phase of growth but did not appear as a result of autolysis of the cells. Maximal lipase synthesis was obtained when the medium was adjusted to pH 7.5 before inoculation. The purified enzyme hydrolyzed tributyrin and tridecanoin most actively, and a relatively high rate of hydrolysis of triolein was also noted. The optimal activity of the purified lipase was at pH 7.5. The characteristics of the concentrated crude enzyme and purified lipase were compared.
D001329:Autolysis; D002118:Calcium / Q000494:pharmacology; D002729:Chloromercuribenzoates / Q000494:pharmacology; D002850:Chromatography, Gel; D003030:Coagulase; D004586:Electrophoresis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000096:biosynthesis* / Q000302:isolation & purification; D012867:Skin / Q000382:microbiology; D012964:Sodium / Q000494:pharmacology; D013210:Staphylococcus / Q000201:enzymology* / Q000254:growth & development; D013696:Temperature; D014280:Triglycerides / Q000378:metabolism
D002729:Chloromercuribenzoates; D003030:Coagulase; D014280:Triglycerides; D012964:Sodium; D008049:Lipase; D002118:Calcium