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  • Electronic Resource  (2)
  • 1990-1994  (2)
  • keratinase purification  (1)
  • sulfhydryl compounds  (1)
  • protease
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  • Electronic Resource  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Keratin degradation by fungi isolated from the grounds of a gelatin factory in Jabalpur, India (1991)
    Springer
    Mycopathologia 114 (1991), S. 83-87 
    Details
    ISSN: 1573-0832
    Keywords: Fungi ; keratin degradation ; sulfhydryl compounds ; sulfate ; thiosulfate ; keratinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The ability of five keratinophilic fungi, i.e., Chrysosporium indicum, Geotrichum candidum, Gymnoascoideus petalosporus, Scopulariopsis brevicaulis, and Talaromyces trachyspermus, to digest human hair keratin in stationary culture has been studied. Degradation of human scalp hair was studied by determination of cysteine, cystine, inorganic sulfate, thiosulfate, total protein, keratinase and change in alkalinity of culture filtrate. Gymnoascoideus petalosporus showed maximum degradation as compared to remaining isolates when grown on human scalp hair as the sole source of nutrients ‘in vitro’.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00436426
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and partial characterization of two extracellular keratinases of Scopulariopsis brevicaulis (1992)
    Springer
    Mycopathologia 119 (1992), S. 161-165 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00448814
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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