Immobilization of lipase from Burkholderia cepacia into calcium carbonate microcapsule and its use for enzymatic reactions in organic and aqueous media

摘要

We disclosed a useful procedure for the immobilization of a lipase from Burkholderia cepacia based on its encapsulation into vaterite calcium carbonate microcapsule. The immobilized enzyme had an adequate activity for the hydrolysis of 4-nitrophenyl acetate, which was preserved over 2 years in storage at 4°C. The enantioselective esteriflcation of (i)-l-phenylethanol with vinyl acetate using the immobilized lipase smoothly progressed to afford the corresponding optically active compounds, where the enzyme was easily recovered for reuse. Although the hydrolysis of (±)-2-acetoxyhexyl tosylate in aqueous solution was catalyzed by the enzyme, the phase transition of calcium carbonate from vaterite to poorly porous calcite during the reaction prevented the access of the reactant to the active site of the lipase, resulting in the significant decrease of the activity of the recovered enzyme. However, the treatment of the immobilized enzyme with zinc chloride solution inhibited the phase transition under the reaction conditions. The enzyme after the zinc treatment was recyclable for the hydrolysis of the substrate without significant decrease of the reactivity even after the uses in aqueous media.