title: Lipase immobilized catalytically active membrane for synthesis of lauryl stearate in a pervaporation membrane reactor.
abstract: A composite catalytically active membrane immobilized with Candida rugosa lipase has been prepared by immersion phase inversion technique for enzymatic synthesis of lauryl stearate in a pervaporation membrane reactor. SEM images showed that a "sandwich-like" membrane structure with a porous lipase-PVA catalytic layer uniformly coated on a polyvinyl alcohol (PVA)/polyethersulfone (PES) bilayer was obtained. Optimum conditions for lipase immobilization in the catalytic layer were determined. The membrane was proved to exhibit superior thermal stability, pH stability and reusability than free lipase under similar conditions. In the case of pervaporation coupled synthesis of lauryl stearate, benefited from in-situ water removal by the membrane, a conversion enhancement of approximately 40% was achieved in comparison to the equilibrium conversion obtained in batch reactors. In addition to conversion enhancement, it was also found that excess water removal by the catalytically active membrane appears to improve activity of the lipase immobilized.
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Membrane Science and Technology, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China. Electronic address: zhangwd@mail.buct.edu.cn.
authors.forename: Weidong
authors.initials: W
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Membrane Science and Technology, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China.
authors.forename: Weihua
authors.initials: W
authors.lastname: Qing
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Membrane Science and Technology, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China.
authors.forename: Zhongqi
authors.initials: Z
authors.lastname: Ren
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Membrane Science and Technology, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China.
authors.forename: Wei
authors.initials: W
authors.lastname: Li
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Membrane Science and Technology, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China.
authors.forename: Jiangrong
authors.initials: J
authors.lastname: Chen
mesh_terms: D055162:Biocatalysis; D019149:Bioreactors; D002175:Candida / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004951:Esterification; D005976:Glutaral / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008567:Membranes, Artificial; D008855:Microscopy, Electron, Scanning; D011142:Polyvinyl Alcohol; D013228:Stearates / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors; D014835:Volatilization
chemical_list: D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D013228:Stearates; D011142:Polyvinyl Alcohol; D008049:Lipase; D005976:Glutaral
keywords: Candida rugosa lipase; Catalytically active membrane; Immersion phase inversion; Lipase immobilization; Pervaporation membrane reactor