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  • 1995-1999  (2)
  • 1960-1964
  • 1995  (2)
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Material
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  • 1995-1999  (2)
  • 1960-1964
Year
  • 1
    Electronic Resource
    Electronic Resource
    Debranching of arabinoxylan: properties of the thermoactive recombinant α-L-arabinofuranosidase from Clostridium stercorarium (ArfB) (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 856-860 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The gene arfB encoding α-L-arabino-furanosidase B of the cellulolytic thermophile Clostridium stercorarium was expressed in Escherichia coli from a 2.2-kb EcoRI DNA fragment. The recombinant gene product ArfB was purified by fast-performance liquid chromatography. It has a tetrameric structure with a monomeric relative molecular mass of 52 00. The optima for temperature and pH are 70 °C and 5.0 respectively. The enzyme appears to have no metal cofactor requirement and is sensitive to sulfhydryl reagents. It hydrolyzes aryl and alkyl α-L-arabinofuranosides and cleaves arabinosyl side-chains from arabinoxylan (oat-spelt xylan) and from xylooligosaccharides produced by recombinant endoxylanase XynA from the same organism. The identity of the N-terminal amino acid sequences indicates that ArfB corresponds to the major α-arabinosidase activity present in the culture supernatant of C. stercorarium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050496
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Debranching of arabinoxylan: properties of the thermoactive recombinant α-L-arabinofuranosidase fromClostridium stercorarium (ArfB) (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 856-860 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The genearfB encoding α-L-arabinofuranosidase B of the cellulolytic thermophileClostridium stercorarium was expressed inEscherichia coli from a 2.2-kbEcoRI DNA fragment. The recombinant gene product ArfB was purified by fast-performance liquid chromatography. It has a tetrameric structure with a monomeric relative molecular mass of 52 00. The optima for temperature and pH are 70°C and 5.0 respectively. The enzyme appears to have no metal cofactor requirement and is sensitive to sulfhydryl reagents. It hydrolyzes aryl and alkyl α-L-arabinofuranosides and cleaves arabinosyl side-chains from arabinoxylan (oat-spelt xylan) and from xylooligosaccharides produced by recombinant endoxylanase XynA from the same organism. The identity of the N-terminal amino acid sequences indicates that ArfB corresponds to the major α-arabinosidase activity present in the culture supernatant ofC. stecorarium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02431919
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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