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  • 1975-1979  (2)
  • Biochemistry and Biotechnology  (2)
  • Camellia japonica
  • ELISA
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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1761-1775 
    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
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 119-128 
    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
    Library Location Call Number Volume/Issue/Year Availability
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