title: Novel magnetic cross-linked lipase aggregates for improving the resolution of (R, S)-2-octanol.
abstract: Novel magnetic cross-linked lipase aggregates were fabricated by immobilizing the cross-linked lipase aggregates onto magnetic particles with a high number of -NH2 terminal groups using p-benzoquinone as the cross-linking agent. At the optimal fabrication conditions, 100% of immobilization efficiency and 139% of activity recovery of the magnetic cross-linked lipase aggregates were achieved. The magnetic cross-linked lipase aggregates were able to efficiently resolve (R, S)-2-octanol, and retained 100% activity and 100% enantioselectivity after 10 cycles of reuse, whereas the cross-linked lipase aggregates only retained about 50% activity and 70% enantioselectivity due to insufficient cross-linking. These results provide a great potential for industrial applications of the magnetic cross-linked lipase aggregates.
authors.affiliation: National Key Laboratory of Biochemical Engineering & Key Laboratory of Green Process Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, P.R. China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Liu
authors.forename: Chen
authors.initials: C
authors.lastname: Guo
authors.forename: Chun-Zhao
authors.initials: CZ
authors.lastname: Liu
mesh_terms: D002384:Catalysis; D003432:Cross-Linking Reagents / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D008280:Magnetics; D000442:Octanols / Q000737:chemistry*; D066329:Protein Aggregates; D013237:Stereoisomerism; D013997:Time Factors
chemical_list: D003432:Cross-Linking Reagents; D000442:Octanols; D066329:Protein Aggregates; C067943:2-octanol; D008049:Lipase
keywords: (R, S)-2-octanol; Yarrowia lipolytica lipase; cross-linked enzyme aggregates; enantioselectivity; immobilization; magnetic nanoparticles