The activity and stability of yeast alcohol dehydrogenase (YADH) entrapped in aerosol OT reverse micellar droplets have been investigated spectrophotometrically. Various physical parameters, e.g., water pool size, w o , pH, and temperature, were optimized for YADH in water/AOT/ isooctane reverse micelles. It was found that the enzyme exhibits maximum activity at wo = 28 and pH 8.1. It was more active in reverse rnicelles than in aqueous buffers at a particular temperature and was denatured at about 30°C in both the systems. At a particular temperature YADH entrapped in reverse micelles was less stable than when it was dissolved in aqueous buffer.
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