| Abstract: | The reactivity of yeast alcohol dehydrogenase (YADH) and horse liver alcohol dehydrogenase (HLADH) towards 12 different aldehydes was tested. YADH was inhibited by pre-incubation with citral, citronellal, p-cuminaldehyde, p-anisaldehyde, m-tolualdehyde, trans-cinnamaldehyde, salicylaldehyde, p-hydroxybenzaldehyde and benzaldehyde, although of these aldehydes only trans-cinnamaldehyde acted as a substrate for the enzyme. HLADH was inhibited, to a much smaller extent, by pre-incubation with citral, salicylaldehyde, citronellal, p-anisaldehyde, piperonaldehyde, trans-cinnamaldehyde, p-hydroxybenzaldehyde and p-cuminaldehyde and all of these aldehydes acted as substrates for the HLADH. Immobilisation of the enzymes on CNBr-activated Sepharose 4B gave protection against inhibition by the aldehydes, suggesting a means of significantly extending the useful lifetime of the enzymes when they are used in industrial processes. |
