ISSN:
0138-4988
Keywords:
Life Sciences
;
Life Sciences (general)
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Glucose dehydrogenase (E.C. 1.1.1.47) from B. megaterium M 1286 was immobilized together with mutarotase (E.C. 5.1.3.3) on several organic carriers and by different methods. The storage stability of the enzyme at pH-values 〉 6 is slightly improved by immobilization and the pH-optimum is shifted from 8.3 to 8.0. Kinetic constants of the immobilized enzyme are: K′M(NAD+) = 5.36 × 10-4 mol/l K′M(glucose) = 3.76 · 10-2 mol/l and V′max = 5.54 · 10-5 mol/(l min g carrier) for the most active preparation (2.16 mg enzyme/g carrier).In reactor experiments the immobilized glucose dehydrogenase was used with glucose to regenerate NADPH in NADPH-dependent iron-III-protoporphyrin-IX-imidazole catalyzed hydroxylation and demethylation of model substrates of cytochrome P-450.The advantages of the coupling of both reactions with cofactor recycling are shown and discussed.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/abio.370060314
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