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  • 1
    Electronic Resource
    Electronic Resource
    Effect of membrane morphology and operation on protein deposition in ultrafiltration membranes (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 47 (1995), S. 174-180 
    Details
    ISSN: 0006-3592
    Keywords: ultrafiltration membranes ; protein fouling ; BET measurements ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Membrane morphology is compared to protein depostion under passive adsorption and ultrafiltration conditions. Solute resistance of protein deposits for membranes of varying roughness, structure, and permeability can vary dramatically with operating conditions. Using Brunauer-Emmett-Teller adsorption isotherm (BET), study of the internal area and accessibility of several uttrafiltration membranes to protein deposition allows better understanding of the fouling mechanisms and interpretation of adsorbed protein quantities. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260470208
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Some factors determining protein aggregation during ultrafiltration (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 260-265 
    Details
    ISSN: 0006-3592
    Keywords: fouling ; ultrafiltration ; protein aggregates ; field emission scanning electron microscopy (FESEM) ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The factors contributing to protein aggregation in albumin ultrafiltration were investigated as a function of operation conditions. The nature of protein deposits was examined by electron microscopy. Protein aggregation appears to occur as a result of rapid supersaturation of protein molecules and high solvent velocity (shear) in the concentrated layer near the membrane surface. The shear occurring in the solvent flow on the membrane surface probably unfolds protein molecules and thus promotes flocculation due to collision between particles. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420216
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    Paper (German National Licenses)
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