オクタデシル化シリカ-ショ糖エステルに固定化したリパーゼの有機溶媒中での酵素活性及びエナンチオ選択性 (<特集>分離・検出と機能物質)

概要

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Three lipases were immobilized on ODS-Sugar, which was prepared by coating sucrose mono-stearate (sugar ester) on octadecvl silica gel (ODS-silica). The enantioselective esterification of (R)- or (S)-1-phenylethanol with aliphatic acid was studied in the presence of immobilized lipase (ODS- Sugar-Lipase) in organic solvents by varying the lipase origin, reaction media and substrate structures. The ODS- Sugar- Lipase (LPL-311) showed both high catalytic activity and enantioselectivity for the esterification of (R)-1-phenylethanol with long-chain aliphatic acid in dry iso-octane. On the other hand, the ODS-Sugar-Lipase (M) showed both a high catalytic activity and enantioselectivity for the esterification of (S)-ibuprofen with hexanol in dry iso-octane. The enzymatic activity of lipases in organic media was remarkably enhanced by immobilization with the sugar ester. The reaction rates of the immobilized lipases were increased by around 100 200-fold compared to that of the native lipases. The activity of the immobilized lipases has been retained for at Ieast one month in refrigerator. The ODS-Sugar-Lipase showed greater activity for ester synthesis than other systems, such as the PEG-grafted lipase and the powder dispersion system. We believe that the ODS-Sugar adsorbed enzyme system can be widely applicable to other enzymes whose substrates are lipophilic.
社団法人日本分析化学会の論文
1999-12-05