Lipase of Malassezia furfur: some properties and their relationship to cell growth.
Lipase activity of Malassezia furfur, detected with alpha-naphthyl palmitate as a substrate, appeared to be associated with the insoluble fraction of the organism. Profiles of M. furfur lipase were similar to those of Candida cylindracea lipase. The pH optimum of the lipase was acidic, pH 5.0, which is very similar to skin surface pH. The enzyme activity was strongly activated by a lipase activator, sodium taurocholate (STC). Addition of STC to the culture medium activated cell growth in a dose-dependent manner and induced hyphae production. These results suggest that M. furfur lipase plays an important role in cell growth.
Ran
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Y
Department of Dermatology, Juntendo University School of Medicine, Tokyo, Japan.
Yoshiike
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T
Ogawa
H
H
D002455:Cell Division / Q000187:drug effects; D003840:Deoxycholic Acid / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D008290:Malassezia / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D012995:Solubility; D013656:Taurocholic Acid / Q000494:pharmacology; D013997:Time Factors
D003840:Deoxycholic Acid; D012967:Sodium Dodecyl Sulfate; D013656:Taurocholic Acid; D008049:Lipase; D004693:Glucan Endo-1,3-beta-D-Glucosidase