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  • 1
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 219-233 
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Experiments were carried out on dextran-dextranase systems to test the prediction of a mechanistic model recently proposed by us, for the synergistic effect of combined exo/endo enzymic action in the degradation of polymeric substrate. Soluble forms of the substrate were used. Preliminary experiments with an insoluble form of the substrate were also carried out to demonstrate the applicability of the analytical techniques to these cases. Molecular weight distributions of the degradation products were determined (by gel-permeation chromatography) and the rates of production of glucose and of other reducing sugars were also measured. It was found that the exodextranase alone had very little effect on the molecular weight distributions compared to a significant shift towards lower molecular weight obtained with the endodextranase which was synergistically enhanced by the action of the combined enzymes. Glucose was produced more rapidly by the exoenzyme compared to the endoenzyme, but combinations of the two enzymes gave a rate enhancement greater than the linear sum of the effects of the two individual enzymes. In comparing the degradation indices and polydispersities of the various degradation products, similar synergistic effects of the combined enzymes in accordance with the theoretical predictions, were observed. The practical implications of these findings to the design of fermentation processes which depend on the action of endo- and exoenzyme mixtures are noted.
    Zusätzliches Material: 10 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1103-1112 
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: β-Galactosidase has been purified from an ammonium sulfate precipitate of E. coli strain ML308 by biospecific adsorption on a column of agarose gel substituted with p-aminophenyl-β-D-thiogalactopyranoside. The system described using a 1.8 liter column has a useful processing capacity of 3.8 × 106 units of β-galactosidase per 2 hr cycle. This corresponds to about 5 g of pure enzyme. An electromechanical timing device operates a set of six solenoid valves and carries out a preset program consisting of sample application, washing, and elation operations.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 583-589 
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Enzymatic properties of Alcaligenes faecalis cells immobilized in polyacrylamide were characterized and compared with those reported for the extracted enzyme, and with those measured for free cells. Many of the properties reflected those of the extracted enzyme rather than those measured in the free whole cells prior to immobilization, suggesting cell disruption during immobilization. These properties included the pH activity profile, a slightly broader pH stability profile, and the activation energy. Electron micrographs showed evidence of cell debris among the polymer matrix. The immobilized cells were not viable, and did not consume glucose. Thermal stability was less after immobilization with a half-life of 16 h at 45°C, and 3.5 h at 50°C. The immobilized preparation was more stable when stored lyophilized rather than in buffer, losing 23 and 52% activity, respectively, after six months. The enzyme was irreversibly inhibited by both acetate and citrate buffers. If the immobilized enzyme is to be used in conjunction with cellulases from Trichoderma reesei for cellulase saccharification, the optimal conditions would be pH 5.5 and 45°C in a buffer containing no carboxylic acid groups.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 623-626 
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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