2003•Acta Scientiarum Naturalium Universitatis SunyatseniRequires access

Stability of Surfactant—coated Candida Rugosa Lipase in Isooctane

宋宝东, 邢爱华, 吴金川, 王世昌

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Abstract

The stability of Candida rugosa lipase coated with glutamic acid didodecyl ester ribitol amide was investigated taking esterification of lauryl alcohol and lauric acid in isooctane as a model reaction.At 30℃,the half-life of the activity of the coated lipase was ca 10h,the enzyme activity became less changed after 12h and the residual activity was 39% of the initial value ,The coated lipase obeyed a first-order deactivation model with a deactivation energy of 29.9 J.mol^-1.

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What this paper is about

The stability of Candida rugosa lipase coated with glutamic acid didodecyl ester ribitol amide was investigated taking esterification of lauryl alcohol and lauric acid in isooctane as a model reaction.At 30℃,the half-life of the activity of the coated lipase was ca 10h,the enzyme activity became less changed after 12h and the residual activity was 39% of the initial value ,The coated lipase obeyed a first-order deactivation model with a deactivation energy of 29.9 J.mol^-1.

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Available abstract

The stability of Candida rugosa lipase coated with glutamic acid didodecyl ester ribitol amide was investigated taking esterification of lauryl alcohol and lauric acid in isooctane as a model reaction.At 30℃,the half-life of the activity of the coated lipase was ca 10h,the enzyme activity became less changed after 12h and the residual activity was 39% of the initial value ,The coated lipase obeyed a first-order deactivation model with a deactivation energy of 29.9 J.mol^-1.

Key concepts: Candida rugosa, Lipase, Lauric acid, Chemistry, Pulmonary surfactant, Alcohol, Triacylglycerol lipase, Organic chemistry

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