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  • 1
    Electronic Resource
    Electronic Resource
    Isolation of β-Xylanase from whole broth of Bacillus amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion (1999)
    Springer
    Bioseparation 8 (1999), S. 273-280 
    Details
    ISSN: 1573-8272
    Keywords: β-1 ; 4-xylanase ; Bacillus amyloliquefaciens ; cation exchanger ; fluidized bed adsorption ; low bed expansion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract β-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3% and purification of 5.3 fold. About 99.99% of the colony forming units, 82% of the contaminating neutral protease activity, and 100% of the reducing sugars present in the crude feedstock were removed at the end of the purification cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008174513826
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Detection of endo-xylanase activities in electrophoretic gels with congo red staining (1995)
    Springer
    Biotechnology techniques 9 (1995), S. 145-148 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A modification of the Congo Red zymographic technique is used to analyse multiple xylanase activities of Bacillus sp. MIR-32 after PAGE and SDS-PAGE. Xylanase activities are associated with at least two major proteins of 18.4 and 19.6 kDa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224415
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Thermal stabilization by polyols of β-xylanase from Bacillus amyloliquefaciens (1998)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 71 (1998), S. 241-245 
    Details
    ISSN: 0268-2575
    Keywords: endo-β-1,4-xylanase ; sorbitol ; polyols ; stabilization ; Bacillus amyloliquefaciens ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Purified endo-β-1,4-xylanase of Bacillus amyloliquefaciens MIR 32 retained 100% of its activity after 4 days of incubation at 50°C. Sorbitol (400 mg cm-3) produced a 63-fold increase in the half-life of the enzyme at 65°C, which was only 29 min at this temperature in the absence of the polyol. This thermal stabilizing activity increased exponentially in respect to sorbitol concentration in the range 250-400 mg cm-3 and was dependent on the pH, showing a maximum at pH values between 5·25 and 8·0. The circular dichroism (CD) thermal scanning profile (50°C h-1) at 224 nm showed that changes in the secondary structure of xylanase started at 65°C, while in the presence of sorbitol (400 mg cm-3) these modifications started at 80°C. This study indicated that sorbitol might be a valuable stabilizer for the use of β-xylanase from B. amyloliquefaciens at high temperatures. © 1998 SCI
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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