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  • keratinase purification  (1)
  • protease  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Characteristics of extracellular proteases produced by Bacillus laterosporus and Flavobacterium sp. isolated from gelatinfactory effluents (1996)
    Springer
    World journal of microbiology and biotechnology 12 (1996), S. 615-617 
    Details
    ISSN: 1573-0972
    Keywords: Bacillus laterosporus ; Flavobacterium ; gelatin ; protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Forty bacterial isolates from the effluents of a gelatin factory (Jabalpur, India) were screened for protease activity and the two most potent producers were identified as Bacillus laterosporus and a Flavobacterium sp. The enzymes of both isolates were optimal at pH 8 and 60°C, with maximum activity after 90 min. The enzyme activity of B. laterosporus was suppressed by Fe2+, Mg2+, Mn2+ and Zn2+ ions but was enhanced by Ba2+ and Ca2+. That of Flavobacterium sp. was suppressed by Mg2+ and Mn2+ ions but enhanced by Ba2+, Ca2+ and Fe2+. The enzyme activity of the former was strongly inhibited by KCN, whereas that of the latter was only slightly inhibited by 8-hydroxyquinoline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327724
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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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