Thermostability of alcohol dehydrogenase in the presence of sucrose

Abstract

SUMIWARYThe influence of sucrose on the thermostability of pure alcohol dehydrogenase is investigated for various temperatures (50-70°C) in the presence and absence of sucrose (0, 80 wt. X). The thermal inactivation clearly exhibits nonlinear biphasic behavior. The thermal inactivation rate constants and the magnitude of the heat-stable and -heat-labile fractions of the enzyme are quantified.