Advertisement

Cofactor Reaction-Diffusion Kinetics for an Alcohol Dehydrogenase Membrane

  • Lemuel B. WingardJr.
  • James R. Millis

Abstract

One approach to an enzyme-catalyzed direct energy transfer device involves diffusion of cofactor from the immobilized enzyme to the solid electrode surface (1). We have studied the kinetics of part of this overall process, using yeast alcohol dehydrogenase (YADH) immobilized in an albumin-glutaraldehyde membrane. Values for the kinetic constants for soluble and immobilized YADH were determined experimentally. These were used to show how the overall rate of reaction was influenced by different degrees of diff-usional resistance of the transport of the cofactor, nicotinamide adenine dinucleotide (NAD).

Keywords

Alcohol Dehydrogenase Immobilize Enzyme Nicotinamide Adenine Dinucleotide Diffusional Resistance Nicotinamide Adenine Dinucleotide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Wingard, Jr., L.B. Hindustan Antibiotics Bull. 20: 109, 1978.Google Scholar
  2. 2.
    Millis, J.R. & Wingard Jr., L.B. (submitted).Google Scholar
  3. 3.
    Dickinson, F.M. & Monger, G.P. Biochem. J.131: 261, 1973.Google Scholar
  4. 4.
    Moo-Young, M. & Kobayashi, T. Can. J. Chem. Eng. 50: 162, 1972.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Lemuel B. WingardJr.
    • 1
  • James R. Millis
    • 1
  1. 1.Department of Pharmacology and Chemical EngineeringUniversity of PittsburghPittsburghUSA

Personalised recommendations