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  • 1
    Electronic Resource
    Electronic Resource
    Preparation of an immobilized two-enzyme system, β-amylase-pullulanase, to an acrylic copolymer for the conversion of starch to maltose. I. Preparation and stability of immobilized β-amylase (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 567-577 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Amylase (EC 3.2.1.2), obtained from barley, was chemically attached to a crosslinked copolymer of acrylamide-acrylic acid using a water-soluble carbodiimide. The derivative showed 23% β-amylase activity in relation to that of free enzyme with a coupling yield of 40% based on the amount of added β-amylase. In order to find optimal coupling conditions, the effect of pH and different carbodiimide concentrations was investigated. The enzymic activity associated with different β-amylase concentrations was further outlined. A slightly increased operational stability for the enzyme upon immobilization was observed. Markedly improved operational stability has been obtained by coupling in the presence of reduced glutathione of bovine serum albumin.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160502
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation of an immobilized two-enzyme system, β-amylase-pullulanase, to an acrylic copolymer for the conversion of starch to maltose. III. Process kinetic studies on continuous reactors (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1567-1587 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Kinetic studies on the parameters influencing the potential industrial application of an immobilized two-enzyme system of β-amylase and pullulanase for conversion of starch to a product with high maltose content, have been performed. The apparent Michaelis constant, the apparent product inhibitor constant, and the activation energy have been determined for the immobilized preparation and compared to the values for the corresponding soluble enzyme system. The catalytic activity of the immobilized enzymes was studied in a plug-flow reactor and a continuous feed stirred tank reactor. Mathematical models for these reactors have been formulated and adapted to fit the experimental data. Comparisons of the reactor efficiencies were made and the conditions were found to be such as to favor the plug-flow reactor. Results on operational stability tests at different temperatures and substrate concentrations are given.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161202
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Covalent coupling of pullulanase to an acrylic copolymer using a water soluble carbodi-imide (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 14 (1972), S. 715-724 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pullulanase (EC 3.2.1.9) prepared from a culture of Acrobacter aerogeneshas been covalently bound to an inert crosslinked copolymer of aerylamide-acrylic acid by using a water-soluble carbodi-imide. The binding yield based on the amount of added pullulanase was 34%. The residual enzymic activity was 43%, of that of free enzyme. Coupling in the presence of the substrate pullulan gave a 5-fold increase in activity over that obtained when substrate was lacking. The effect of different carbodi-imide concentrations on the coupling has been investigated. The isoelectric point of the pullulanase preparation (3.5-4.0) was determined using isoelectric, focusing, in order to find optimal pH conditions for the coupling procedure. The immobilized pullulanase in a packed bed column was used to debranch amylopeetin to low molecular weight amylose.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260140503
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Preparation of an immobilized two-enzyme system, β-amylase-pullulanase, to an acrylic copolymer for the conversion of starch to maltose. II. Cocoupling of the enzymes and use in a packed bed column (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 579-591 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Amylase (EC 3.2.1.2) and pullulanase (EC 3.2.1.9) have been covalently bound in a two-enzyme system to a crosslinked copolymer of acrylarmide-acrylic acid by using a water-soluble carbodiimide. The coupling yields based on the amounts of added β-amylase and pullulanase were 40% and 38%, respectively, with residual enzymic activities of 22% and 32% of those of free enzymes. A markedly increased operational stability was observed for the immobilized two-enzyme system compared to the free enzymes in solution. In order to find optimal operational conditions the influence of different pH values and temperatures on the conversion process was investigated. The action of the immobilized β-amylase-pullulanase derivative on partially hydrolyzed starch (DE 3.4-10.7) in a packed bed column was studied. Analysis of the product was performed using gas-liquid chromatography.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160503
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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