Korean J Med Mycol.  2007 Mar;12(1):9-17.

The Enzymatic Approach of Zygomycosis - Causing Mucorales

Affiliations
  • 1Center for Traditional Microorganism Resources, Keimyung University, Dalseo-gu, Daegu 704-701, Korea.
  • 2Research Center for Pathogenic Fungi and Microbial Toxicoses,Chiba University, Chiba 260-8673, Japan.
  • 3Department of Microbiology, Collage of Natural Science, Keimyung University, Dalseo-gu, Daegu 704-701, Korea. hskim@kmu.ac.kr

Abstract

Various oxidases and hydrolytic enzymes were analyzed to investigate the relationship between these enzymes and the skin pathogenicity of 18 Mucorales strains. Each strain was cultured in a nutrient medium containing starch as a carbon source. The cells grew quickly and were at a good state of growth after incubation for three days. Oxidase activity was not detected in any strain, whereas Mucor spp. including Mucor racemosus IFM47053 typically had high alcohol dehydrogenase (ADH) activity and all the strains had catalase activity. The culture filtrate and the cell free extract of each strain were applied to APIZYM test system, which revealed that all the strains examined produced many hydrolytic enzymes both inside and outside their mycelia. In the case of Absidia corymbifera strains, lipase activity was comparatively high, and polysaccharide hydrolytic enzymes such as alpha-glucosidase, beta-glucosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and alpha-fucosidase were produced.

Keyword

Zygomycosis; Alcohol dehydrogenase (ADH); Catalase; Hydrolases

MeSH Terms

Absidia
Alcohol Dehydrogenase
alpha-Glucosidases
alpha-L-Fucosidase
alpha-Mannosidase
beta-Glucosidase
Carbon
Catalase
Hydrolases
Lipase
Mucor
Mucorales*
Oxidoreductases
Skin
Starch
Virulence
Zygomycosis*
Alcohol Dehydrogenase
Carbon
Catalase
Hydrolases
Lipase
Oxidoreductases
Starch
alpha-Glucosidases
alpha-L-Fucosidase
alpha-Mannosidase
beta-Glucosidase
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