title: Immobilizing Yarrowia lipolytica Lipase Lip2 via Improvement of Microspheres by Gelatin Modification.
abstract: The purpose of this study was to investigate the feasibility of immobilizing Yarrowia lipolytica lipase lip2 on epoxy microspheres with or without gelatin modifications. The activity of lipase immobilized on gelatin-modified supports was twofold higher than those immobilized on native supports. There was no significant difference in the Michaelis-Menten constant (K M ) between the two immobilized lipases. However, lipase immobilized on gelatin modified supports showed an approximately fourfold higher V max than lipase immobilized on native supports. Lipase immobilization on the gelatin-modified support exhibited a significantly improved operational stability in an esterification system. After it was reused for a total of 35 batches, the ester conversion of lipase immobilized on gelatin-modified and native microspheres was 83 and 60 %, respectively. Furthermore, the immobilized lipase could be stored at 4 °C for 12 months without any loss of activity.
authors.affiliation: National Energy R&D Center for Biorefinery, Beijing Key Laboratory of Bioprocess, College of Biology Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
authors.forename: Rong
authors.initials: R
authors.lastname: Xie
authors.affiliation: National Energy R&D Center for Biorefinery, Beijing Key Laboratory of Bioprocess, College of Biology Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
authors.forename: Caixia
authors.initials: C
authors.lastname: Cui
authors.affiliation: National Energy R&D Center for Biorefinery, Beijing Key Laboratory of Bioprocess, College of Biology Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China. chenbiqiang@gmail.com.
authors.forename: Biqiang
authors.initials: B
authors.lastname: Chen
authors.affiliation: National Energy R&D Center for Biorefinery, Beijing Key Laboratory of Bioprocess, College of Biology Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
authors.forename: Tianwei
authors.initials: T
authors.lastname: Tan
mesh_terms: D055162:Biocatalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D005240:Feasibility Studies; D005780:Gelatin / Q000737:chemistry*; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008863:Microspheres; D025062:Yarrowia / Q000201:enzymology*
chemical_list: D004800:Enzymes, Immobilized; D005780:Gelatin; D008049:Lipase
keywords: Gelatin; Immobilization; Lipase; Microsphere; Modification