Matthew W. Eggert, Department of Chemical Engineering, Auburn University, 170 Wilmore, Auburn, AL 36849-5127, Mark E. Byrne, Biomimetic & Biohybrid Materials, Biomedical Devices, and Drug Delivery Laboratories, Department of Chemical Engineering, Auburn University, 324 Ross Hall, Auburn, AL 36849-5127, and Robert P. Chambers, Chemical Engineering, Auburn University, 240 Ross Hall, Auburn, AL 36849-5127.
For the purpose of improving the rate of alcohol metabolism within the human body, a multi-enzyme system containing alcohol (ADH), acetaldehyde (ALDH) and lactic (LDH) dehydrogenases, linked together by cofactor NAD, is currently being investigated. Three enzyme experiments show rapid metabolism of ethanol while maintaining potentially toxic acetaldehyde well below harmful concentrations. Efficient conversion of ethanol to non-toxic acetate, reduction of inhibition effects, and regeneration of cofactor NAD highlight the abilities of the multi-enzyme system. Using a multi-enzyme simulation model in conjunction with experimental data, effective relative amounts of each enzyme were determined for achieving a high overall rate of ethanol conversion.
Studies of covalently bound alcohol dehydrogenase onto a polymer matrix have been performed via UV free-radical polymerization following functionalization of the enzyme amino groups with acryloyl chloride. Enzyme activity, based on initial rate kinetics, beginning with the free enzyme through functionalization then polymerization is monitored. UV exposure is minimized to prevent denaturization of enzyme. Up to 40% ADH enzyme activity is retained in gel form. Experimental diffusion characteristics indicate sufficient transport for an effective matrix bound enzyme system.