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  • Electronic Resource  (3)
  • Eudragit S-100  (1)
  • fluidized bed adsorption  (1)
  • lysozyme  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Protein separation using metal ion-bound particles in aqueous two-phase system (1999)
    Springer
    Biotechnology techniques 13 (1999), S. 145-148 
    Details
    ISSN: 1573-6784
    Keywords: protein separation ; aqueous two-phase system ; affinity partitioning ; lysozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Metal ion affinity partitioning of protein in aqueous two-phase systems was studied using Sepharose as ligand carrier as an integrated adsorption partitioning. Cu(II)-bound Sepharose was mixed with protein solution and an aqueous two-phase system. The affinity sorbent was distributed quantitatively to the upper side or the interface. The binding studies of lysozyme to copper-bound gel in PEG/dextran two-phase systems demonstrate the feasibility of this bioseparation process. PEG/dextran system did not affect binding and elution of lysozyme to and from the Cu(II)-Sepharose particles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008943624956
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Recovery of a monoclonal antibody from hybridoma culture supernatant by affinity precipitation with Eudragit S-100 (2000)
    Springer
    Bioseparation 9 (2000), S. 291-298 
    Details
    ISSN: 1573-8272
    Keywords: affinity precipitation ; Eudragit S-100 ; monoclonal antibodies ; purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An IgG1 monoclonal antibody (MAB) was isolated from hybridoma culture supernatant by affinity precipitation with an Eudragit S-100-based heterobifunctional ligand. Affinity binding was performed in a homogeneous aqueous phase at pH 7.5 followed by precipitation of the bound affinity complex by lowering the pH to 4.8. After two washing steps, elution of specifically bound MAB was achieved by incubating the precipitate with 0.1 M glycine.HCl pH 2.5. The influence of elution volume and time on the recovery of active MAB and the overall purification factor were studied. The best conditions enabled the recovery of 50.2% of active MAB with a purification factor of 6.2. A further dialysis against 50 mM Tris.HCl pH 8.0 increased the activity yield and the purification factor to 68.4% and 8.3, respectively. This result showed that part of the antibody activity loss during affinity precipitation was due to a reversible inactivation process, being easily recovered after a refining dialysis step.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1011183904966
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    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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