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  • 1
    Electronic Resource
    Electronic Resource
    Application of polylysine bound succinyl-NA to a membrane reactor (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1761-1775 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The amide bond at N-6 in succinyl-NAD was found to be more stable than in former accounts. Succinyl-NAD was coupled on polylysine to give a new polymer derivative of NAD, which retained at least 85% of the initial coenzymic activity even after dialysis for one week. The polymer derivative of NAD could be applied to a membrane reactor containing alcohol dehydrogenase and lactate dehydrogenase and lactate was continuously produced in a half-life of ten days.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181210
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation of immobilized enzymes from acrylic monomers under γ-ray irradiation (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 119-128 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized glucoamylase, invertase, and β-galactosidase were prepared by using 2-hydroxyethyl acrylate and dimethylacrylamide under γ-ray irradiation. In the case of 2-hydroxyethyl acrylate, the monomer-enzyme solution was changed to the gel by irradiation of less than 1.0 Mrad, but it was difficult to eliminate enzyme leakage from the gel. When leakage was eliminated by increased irradiation, the activities of the gels were very low. In the case of dimethylacrylamide, the monomer-enzyme solution was changed to a gel by irradiation of 1.0 Mrad; leakage could be eliminated by irradiation of 2.0 Mrad. This gel possessed very high activity. In the case of acrylic acid-sodium acrylate, the monomer-enzyme solution could not be changed to a gel. In preparing gels, high concentrations of enzyme protein had a tendency to obstruct gelation.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260170110
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Preparation of immobilized enzymes by N-Vinylpyrrolidone and the general properties of the glucoamylase gel (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1517-1528 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized glucoamylase, invertase, and β-galactosidase were prepared by using N-vinylpyrrolidone monomer (VP) under γ-ray irradiation. The enzyme-VP solutions were gelled by irradiation with 2.9 Mrad and the added enzymes were almost completely entrapped. Activity losses on entrapping were 55% for the VP-glucoamylase gel, and more than 90% in the case of VP-invertase and VP-β-galactosidase gels. No leakage of enzyme from these gels could be detected within 1 hr. The VP-glucoamylase gel was capable of hydrolyzing dextrin (mol wt 10,400) to glucose and the glucose equivalent was equal to that obtain able with native enzyme. The optimum temperature, heat stability, pH activity curve, and pH stability of VP-glucoamylase gel were slightly inferior to those of native enzyme, while Km was a little larger than that of native enzyme.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161108
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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