Effects of trehalose on pressure-induced inactivation of yeast alcohol dehydrogenase

Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures (<3 kbar). The time courses for inactivation are biphasic and both phases of both isozymes are protected by trehalose. ADH-I is slightly more barostable than ADH-II which is opposite to their thermostabilities. Trehalose at 1M extends their half-lives about 6-fold at 2 kbar, pH 7.5 and 25 degrees C. In contrast, 1M sucrose provides only 4.4-fold protection under identical conditions, a finding consistent with the superior protein stabilization of trehalose to other denaturants.