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  • Electronic Resource  (2)
  • 1990-1994  (2)
  • cystine  (1)
  • keratinase purification  (1)
  • protease
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  • Electronic Resource  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Mycopathologia 118 (1992), S. 147-152 
    ISSN: 1573-0832
    Keywords: Fungi ; cystine ; sulfitolysis ; sulfate ; thiosulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Twenty-six different species of keratinophilic fungi were examined to determine their ability to utilize free cystine. Of the fungi tested, the majority metabolized free L-cystine in a glucose-peptone culture medium. Cystine was used as source of sulfur, and carbon and nitrogen as well. Excess sulfur was excreted into the culture fluid, as thiosulfate and sulfate, following oxidation. The rate of cystine oxidation varied with the different fungal strains, but was maximal for Graphium penicilloideus (88.5%). Low quantities of thiols were found in the medium. Cystine oxidation and inorganic thiosulfate excretion were found to correlate significantly (r = 0.94).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-0832
    Keywords: S. brevicaulis ; keratinase purification ; partial characterization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Two extracellular keratinases of Scopulariopsis brevicaulis were purified and partially characterized. The enzymes were isolated by the techniques of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These keratinases (K I & K II) were purified approximately 33 and 29 fold, respectively. SDS-PAGE of the products of gel filtration chromatography (K I & II) produced only one band each, suggesting homogeneity. The optimum pH for both keratinases was 7.8, while the optimum temperatures were 40°C (K I) and 35°C (K II). Estimated molecular weights were 40–45 KDa and 24–29 KDa for K I & K II respectively. Both keratinases were inhibited by phenylmethylsulfonyl fluoride which suggests a serine residue at or near an active site.
    Type of Medium: Electronic Resource
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