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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 54 (1988), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Microbial degradation of native cellulose to glucose is catalysed by cellulases which refers to a group of enzymes acting in concert. The extracellular enzyme systems of Trichoderma reesei, Sporotrichum pulverulentum, Aspergillus niger and Sclerotium rolfsii have been examined more extensively than other microbial sources. The objective of this review is to present a comparative study of the research on cellulase and hemicellulase enzymes from S. rolfsii.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology techniques 11 (1997), S. 589-591 
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The rates of hydrolysis by b-D-glucosidase, b-D-xylosidase and a-L-arabinofuranosidase isolated from Sclerotium rolfsii were increased 17 to 220 fold in organic solvents as compared to aqueous system with the highest rates occurring in chlorinated hydrocarbons. The molecular weight, log P, Hildebrand solubility parameter and dielectric constant of the solvents correlated with the activities of glycosidases.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology techniques 8 (1994), S. 681-682 
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Provision of a side arm to the miniscale electrofocusing unit facilitated easy collection of protein samples without disturbing the density and pH gradients. This unit required low amounts of carrier electrolytes due to the improved dimensions of the U-tube assembly.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1832-1837 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Extracellular β-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) from culture filtrates of Neurospora crassa was purified to homogeneity by preparative isoelectric focusing followed by gel electrophoresis. The molecular weight of the purified xylosidase was 83,000 D and the Km on p-nitrophenyl-β-D-xyloside was 0.047mM. The homogeneous xylanase (1,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) and β-xylosidase showed differences in their mode of action towards xylooligosaccharides. The degree of hydrolysis of D-xylan by xylanase of N. crassa was 18%. Supplementation of β-xylosidase from the same organism resulted in 48% hydrolysis. The synergistic effect was more pronounced, with the hydrolysis of 68%, when a homogeneous preparation of β-xylosidase from Sclerotium rolfsii was added to the saccharification system.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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