Abstract
This work studies safflower oil hydrolysis catalyzed by Candida rugosa lipase as a function of temperature in an oil-in-water emulsion stabilized by the surfactant sodium deoxycholate. The choice of temperature for this reaction is dictated by the effects of temperature not only on the catalytic activity and stability of the enzyme but also on the state of the reaction medium (emulsion), whose quality substantially affects both the kinetic parameters of lipase and the product (linoleic acid) yield. For example, although the highest initial rate of the enzymatic reaction is observed at 40°C and the enzyme is virtually not inactivated during incubation (45°C), the highest reaction yield is observed at 30°C and decreases upon temperature elevation because of a change in the emulsion quality.
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