Abstract
Bacillus subtilis, containing a stereospecific esterase, and isolated pig liver esterase have been used to hydrolyse menthyl acetate in aqueous-organic media in 50- or 75-ml stirred reactors, respectively. Whereas the stability of the B. subtilis esterase was unaffected by intense agitation, stirrer speeds above 1,000 rev min −1 caused a loss of pig liver esterase activity. Both biocatalysts gave reduced product formation rates when present at high concentrations because of substrate mass transfer limitation. Finally, the B. subtilis esterase showed maximum activity at a phase ratio of 0.5–0.6. For the isolated esterase, use of high phase ratios caused a loss of activity with time, but low phase ratios afforded maximum reaction rates.
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