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Partial characterization of the extracellular keratinase from Microsporum canis
Sabouraudia
|January 1, 1984
Abstract:
The extracellular keratinase of Microsporum canis released peptides from alpha-type fibrous protein and the membranous fraction isolated from human stratum corneum. Inhibition of the enzyme by phenylmethyl-sulfonylfluoride and its weak inhibition by N-ethylmaleimide and etheneglycol tetra-acetic acid indicated that it is probably a serine proteinase.
Insights
Microsporum canis releases peptides from human skin proteins using an extracellular enzyme. This enzyme is likely a serine proteinase, as indicated by its inhibition patterns.
Area of Science:
- Biochemistry
- Dermatology
- Microbiology
Background:
- Extracellular enzymes play crucial roles in microbial pathogenesis and nutrient acquisition.
- The human stratum corneum, a protective outer layer, contains fibrous proteins like keratin.
Purpose of the Study:
- To investigate the substrate specificity and enzymatic properties of the extracellular keratinase from Microsporum canis.
- To characterize the enzyme's potential as a serine proteinase.
Main Methods:
- Incubation of alpha-type fibrous protein and human stratum corneum fractions with Microsporum canis extracellular keratinase.
- Enzyme inhibition assays using phenylmethyl-sulfonylfluoride (PMSF), N-ethylmaleimide (NEM), and ethylene glycol tetra-acetic acid (EGTA).
Main Results:
- The keratinase released peptides from both alpha-type fibrous protein and the membranous fraction of human stratum corneum.
- Phenylmethyl-sulfonylfluoride strongly inhibited the enzyme.
- N-ethylmaleimide and ethylene glycol tetra-acetic acid showed weak inhibition, suggesting a serine proteinase mechanism.
Conclusions:
- Microsporum canis extracellular keratinase effectively degrades human stratum corneum components.
- The enzyme's inhibition profile strongly suggests it is a serine proteinase, relevant for understanding fungal-host interactions.