Lipase of Malassezia furfur: some properties and their relationship to cell growth
Y Ran, T Yoshiike, H Ogawa - Journal of medical and veterinary …, 1993 - Taylor & Francis
Y Ran, T Yoshiike, H Ogawa
Journal of medical and veterinary mycology, 1993•Taylor & FrancisLipase activity of Malassezia furfur, detected with a-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 …
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 …
Lipase activity of Malassezia furfur, detected with a-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.
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