Abstract
In order to establish a more general mechanism of enzyme stabilization, it is necessary to study the behavior of other types of enzymes in the presence of various additives. The effect of different additives (polyhydric alcohols, polyethylene glycol and salts) on the thermostability of Trichoderma viride cellulase at 60 ℃ was studied in aqueous medium. The results showed that the effect was stabilized in the presence of polyhydric alcohols (ethylene glycol, glycerol, erythritol, xylitol and sorbitol) and most of the polyethylene glycol. The effect of the monovalent ions on cellulase thermostability could be correlated to the lyotropic series of Hofmeister. The thermal denaturation of cellulase was performed in a 97% deuterium water medium. In this medium, the enzyme was more stable and its half life was 2.6-fold higher than that in normal water. Considering the results obtained with cellulase stability in the presence of polyhydrie alcohols, PEG, salts and D2O, it is possible to propose a more general mechanism of enzyme stabilization.
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