Stability of Surfactant-coated Candida Rugosa Lipase in Isooctane
Jinchuan Wu
Abstract
Jinchuan Wu
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 30C, the half-life of the activity of the coated lipase was ca 10 h, the enzyme activity became less changed after 12 h and the residual activity was 39% of the initial value. The coated lipase obeyed a first-order deactivation model with a deactivation energy of 29.9J.mol-1.
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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 30C, the half-life of the activity of the coated lipase was ca 10 h, the enzyme activity became less changed after 12 h and the residual activity was 39% of the initial value. The coated lipase obeyed a first-order deactivation model with a deactivation energy of 29.9J.mol-1.
Key concepts: Candida rugosa, Lipase, Lauric acid, Chemistry, Pulmonary surfactant, Alcohol, Heat stability, Triacylglycerol lipase