The surfactant-coated Candida rugosa lipase was used as catalyst for hydrolysis of olive oil in two-phase system consisting of olive oil and phosphate buffer without organic solvent. For both the coated and native lip...The surfactant-coated Candida rugosa lipase was used as catalyst for hydrolysis of olive oil in two-phase system consisting of olive oil and phosphate buffer without organic solvent. For both the coated and native lipases,the optimal buffer/oil volume ratio of 1.0, aqueous pH 6.8 and reaction temperature 30℃ were determined. The maximum activity of the coated lipase was ca 1.3 times than that of the native lipase. The half-life of the coated lipase in olive oil and the native lipase in phosphate buffer was ca 9 h and 12 h, and the final residual activity was 27% and 20% of their initial values, respectively. The final substrate conversion by the coated lipase was ca 20% higher than that of the native lipase.展开更多
An efficient lipase-catalyzed enantioselective hydrolysis of bu-tyryloxyalkanephosphonates in water-equilibrated diisopropyl ether was developed. The relationship between the substrates' structure and the reactivi...An efficient lipase-catalyzed enantioselective hydrolysis of bu-tyryloxyalkanephosphonates in water-equilibrated diisopropyl ether was developed. The relationship between the substrates' structure and the reactivity, as well as the enantioselectivity of this enzymatic transformation was studied. The catalytic preference of crude Candida rugosa lipase toward such molecules was assigned according to modified Mosher's method and X-ray crystallographic analysis. Optically pure 2-hydroxy-2-arylethanephosphonates, 3-hydroxy-3-phenylpropanephosphon-ate, and 3,3,3-trifluoro-2-hydroxypropanephosphonates were conveniently prepared in this manner.展开更多
基金National Natural Science Foundation of China(No.29876031)
文摘The surfactant-coated Candida rugosa lipase was used as catalyst for hydrolysis of olive oil in two-phase system consisting of olive oil and phosphate buffer without organic solvent. For both the coated and native lipases,the optimal buffer/oil volume ratio of 1.0, aqueous pH 6.8 and reaction temperature 30℃ were determined. The maximum activity of the coated lipase was ca 1.3 times than that of the native lipase. The half-life of the coated lipase in olive oil and the native lipase in phosphate buffer was ca 9 h and 12 h, and the final residual activity was 27% and 20% of their initial values, respectively. The final substrate conversion by the coated lipase was ca 20% higher than that of the native lipase.
基金Project supported by the National Natural Science Foundation of China(Nos.20272075,20072052).
文摘An efficient lipase-catalyzed enantioselective hydrolysis of bu-tyryloxyalkanephosphonates in water-equilibrated diisopropyl ether was developed. The relationship between the substrates' structure and the reactivity, as well as the enantioselectivity of this enzymatic transformation was studied. The catalytic preference of crude Candida rugosa lipase toward such molecules was assigned according to modified Mosher's method and X-ray crystallographic analysis. Optically pure 2-hydroxy-2-arylethanephosphonates, 3-hydroxy-3-phenylpropanephosphon-ate, and 3,3,3-trifluoro-2-hydroxypropanephosphonates were conveniently prepared in this manner.
