Abstract
The capacities of yeast wild-type and mutants strains known to lack specific ADH isoenzymes to produce L-phenylacetyl carbinol (PAC) and benzyl alcohol in biotransformation trials were also investigated. Pyruvate decarboxylase activity, responsible for PAC formation and ADH activity, which can participate in reduction of benzaldehyde to benzyl alcohol, was also determined in each strain. In addition, the capacity of each strain to produce ethanol was investigated. Mutant strains lacking all of the isoenzymes, ADH-I, ADH-II, and ADH-III, still exhibited some ADH activity and were capable of production of benzyl alcohol and ethanol.
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