Multiple forms and functions of Candida rugosa lipase
Rey-Chang Chang, Shu‐Jen Chou, Jei‐Fu Shaw
Abstract
Rey-Chang Chang, Shu‐Jen Chou, Jei‐Fu Shaw
Abstract
The PAGE patterns of lipolytic enzymes obtained from three commercial Candida rugosa lipases differed. The difference in protein composition would account for the difference in the catalytic efficiency and specificity of Candida rugosa lipase reported in the literature. The presence of Tween 80 and Tween 20 in the culture medium not only promoted the lipase productivity, but also changed the production of multiple forms in cultured Candida rugosa. These lipase preparations showed quite different substrate specificities and thermal stabilities. The results suggest that the specificity and stability of lipase preparations used in biotechnological applications can be modulated by culture conditions which change the multiple-form compositions
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The PAGE patterns of lipolytic enzymes obtained from three commercial Candida rugosa lipases differed. The difference in protein composition would account for the difference in the catalytic efficiency and specificity of Candida rugosa lipase reported in the literature. The presence of Tween 80 and Tween 20 in the culture medium not only promoted the lipase productivity, but also changed the production of multiple forms in cultured Candida rugosa. These lipase preparations showed quite different substrate specificities and thermal stabilities. The results suggest that the specificity and stability of lipase preparations used in biotechnological applications can be modulated by culture conditions which change the multiple-form compositions
Key concepts: Candida rugosa, Lipase, Rugosa, Enzyme, Biochemistry, Substrate (aquarium), Substrate specificity, Triacylglycerol lipase