Horse liver alcohol dehydrogenase, which catalyzes oxidoreductions for a broad spectrum of substrates of organic chemical interest, was immobilized on CNBr-activated Sepharose and on decylamine-substituted agarose. The specific activities of the immobilized enzyme preparations were compared with the free enzyme, and the apparent K(m) values of the preparations were determined for a selection of substrates. At pH 9 and 60 degrees C, soluble liver alcohol dehydrogenase was rapidly inactivated, while the enzyme immobilized on CNBr-activated Sepharose was more stable. Adenosine monophosphate (AMP), adenosine diphosphate, and adenosine diphosphoribose protected the free and immobilized alcohol dehydrogenase against heat inactivation. On storage under a variety of conditions, AMP effectively stabilized free horse liver alcohol dehydrogenase and the immobilized preparations.
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Görisch et al. (1984) studied this question.
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