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- W2588894678 abstract "The effect of trehalose (0.5 M) on the thermal stability of cutinase in the alkaline pH range was studied. The thermal unfolding induced by increasing tempera- ture was analyzed in the absence and in the presence of trehalose according to a two-state model (which as- sumes that only the folded and unfolded states of cutin- ase were present). Trehalose delays the reversible un- folding. The midpoint temperature of the unfolding tran- sition (Tm) increases by 4.0°C and 2.6°C at pH 9.2 and 10.5, respectively, in the presence of trehalose. At pH 9.2 the thermal unfolding occurs at higher temperatures (Tm is 52.6°C compared to 42.0°C at pH 10.5) and a refolding yield of around 80% was obtained upon cooling. This pH value was chosen to study the irreversible inactivation (long-term stability) of cutinase. Temperatures in the transition range from folded to unfolded state were se- lected and the rate constants of irreversible inactivation determined. Inactivation followed first-order kinetics and trehalose reduced the observed rate constants of inacti- vation, pointing to a stabilizing effect on the irreversible inactivation step of thermal denaturation. However, if the contribution of reversible unfolding on the irreversible inactivation of cutinase was taken into account, i.e., con- sidering the fraction of cutinase molecules in the revers- ible unfolded conformation, the intrinsic rate constants can be calculated. Based on the intrinsic rate constants it was concluded that trehalose does not delay the irrevers- ible inactivation. This conclusion was further supported by comparing the activation energy of the irreversible inactivation in the absence and in the presence of treha- lose. The apparent activation energy in the absence and in the presence of trehalose were 67 and 99 Kcal/mol, respectively. The activation energy calculated from in- trinsic rate constants was higher in the absence (30 Kcal/ mol) than in the presence of trehalose (16 Kcal/mol), showing that kinetics of the irreversible inactivation step increased in the presence of trehalose. In fact, trehalose stabilized only the reversible step of thermal denatur- ation of cutinase. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 70: 699-703, 2000." @default.
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- W2588894678 title "COMMUNICATION TO THE EDITOR Trehalose Delays the Reversible But Not the Irreversible Thermal Denaturation of Cutinase" @default.
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