Cited by 53Nail Diseases and TreatmentsEnzyme Production and CharacterizationFungal and yeast genetics research

Characterization of the lipase activity of Malassezia furfur

Plotkin, L.I., Squiquera, L., Mathov, I., Galimberti, R., Leoni, J.·1996·Medical Mycology

Abstract

Enzymes capable of metabolizing lipids are essential for the growth of Malassezia furfur in vitro and in vivo. We designed a series of experiments to characterize the lipolytic system in this yeast. The optimal pH of the lipase system was 7.5 Lipase activity was detected in soluble and insoluble saline cell extracts and in supernatant from the cultures. Esterase activity screened in samples separated by native polyacrylamide gels showed that it was restricted to one band of low mobility. An FPLC analysis of the soluble saline extract demonstrated that the lipase activity was present in three major peaks with different protein composition as revealed by SDS-PAGE. The enzymatic activity and cell growth were first induced and later inhibited by increasing concentrations of polyethylene-sorbitan-monooleate (Tween-80). The characterization of the lipolytic system (e.g. its induction by substrate and the effect of pH and/or different cations) could help to explain the increment in the number of M. furfur infections related to alterations of surface lipids in the skin such as seborrheic dermatitis.

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Registry

Crossref · 10.1080/02681219680000071

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  • Malassezia has lipase activity, which hydrolyzes human sebum triglycerides and releases unsaturated fatty acids such as oleic and arachidonic acid.

    “Furthermore, Malassezia was shown to have lipase activity, which hydrolyzes human sebum triglycerides and releases unsaturated fatty acids such as oleic and arachidonic acid [51,52].”

    From Seborrheic Dermatitis and Dandruff: A Comprehensive Review (2015) · cites this paper as [52]

    The Abstract and Discussion report lipase activity in Malassezia furfur, and the Titrimetric determination of lipase section measures fatty acids formed by hydrolysis of olive oil (page numbers unavailable). The paper does not establish that the enzyme hydrolyzes human sebum triglycerides or releases oleic and arachidonic acids specifically. (LLM, conf=0.90)

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Research works printed but not linked: 1

  1. Faegermann J, 1985, Semin Dermatol, 4, 173

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Authors
Plotkin, L. I., Squiquera, L., Mathov, I., Galimberti, R., & Leoni, J.
Affiliations
  • Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
  • Hospital Italiano de Buenos Aires (AR)
Venue
Medical Mycology
Published
1996-01
Volume
34
Issue
1
Pages
43-48
ISSN
  • 0268-1218 (ISSN-L)
  • 1369-3786
  • 1460-2709
OpenAlex
W1986688279
Cited by
53
References
21
Citations by year
2025: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 4 · 2019: 6 · 2017: 1 · 2015: 4 · 2014: 1 · 2013: 2 · 2012: 1
FWCI
0.97
Type
journal article
Language
en
Open access
closed
Locations
  • Medical Mycology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Epidemiology › Nail Diseases and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
Malassezia furfur, lipase activity, esterase activity, lipid metabolism, pH optimum, enzyme purification, seborrheic dermatitis, yeast lipase
MeSH terms
Chromatography, Liquid, Esterases, Hydrogen-Ion Concentration, Lipase, Malassezia

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