Cofactor Reaction-Diffusion Kinetics for an Alcohol Dehydrogenase Membrane

  • Lemuel B. WingardJr.
  • James R. Millis


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).


Alcohol Dehydrogenase Immobilize Enzyme Nicotinamide Adenine Dinucleotide Diffusional Resistance Nicotinamide Adenine Dinucleotide 
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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

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