Kinetic and modelling studies on the lipase catalysed enantioselective esterification of (±)-perillyl alcohol
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- 作者：Skouridou ; Vasso ; Chrysina ; Evangelia D. ; Stamatis ; Haralambos ; Oikonomakos ; Nikos G. ; Kolisis ; Fragiskos N.
- 关键词：AoL ; Aspergillus oryzae lipase ; CALB ; Candida antarctica lipase B ; CcL ; Candida cylindracea lipase ; ClL ; Candida lipolytica lipase ; MjL ; Mucor javanicus lipase ; RmL ; Rhizomucor miehei lipase ; PrL ; Penicillium roqueforti lipase ; PPL ; porcine pancreas lipas
- 刊名：Journal of Molecular Catalysis B: Enzymatic
- 出版年：2004
- 出版时间：June 21, 2004
- 年：2004
- 卷：29
- 期：1-6
- 页码：9-12
- 全文大小：113 K
文摘
Several lipases were kinetically studied with the aim to exploit their enantioselectivity in the esterification of (S)-(−) and (R)-(+)-perillyl alcohol with decanoic acid. Most of the lipases studied exhibited stereopreference towards the R-enantiomer with apparent E-values from 3.8 to 0.6, calculated as the initial esterification rates ratio for the individual enantiomers. In an attempt to interpret the structural basis of enantioselectivity, modelling studies were performed with two of these lipases, Candida cylindracea lipase (CcL) and Pseudomonas cepacia lipase (PcL) based on their previously determined X-ray crystal structures. The results derived from modelling studies confirm their stereopreferences towards the R-enantiomer, since increased conformational energy of the S-ester was found compared to the R-ester.