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Activity and stability of yeast alcohol dehydrogenase (YADH) entrapped in aerosol OT reverse micelles
Author(s) -
Sarcar Shraboni,
Jain Tanoj Kumar,
Maitra Amarnath
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260390416
Subject(s) - micelle , chemistry , aqueous solution , chromatography , alcohol dehydrogenase , yeast , alcohol , buffer solution , aerosol , nuclear chemistry , organic chemistry , biochemistry
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 0 , pH, and temperature, were optimized for YADH in water/AOT/isooctane reverse micelles. It was found that the enzyme exhibits maximum activity at w 0 = 28 and pH 8.1. It was more active in reverse micelles than in aqueous buffers at a particular temperature and was denatured at about 307deg;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.