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Immobilization of lipase onto metal-organic frameworks for enantioselective hydrolysis and transesterification
  • +3
  • Xin Yuan,
  • Yu Liu,
  • Fan Cao,
  • panliang zhang,
  • Jian Ou,
  • Kewen Tang
Xin Yuan
Hunan Institute of Science and Technology
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Yu Liu
Hunan Institute of Science and Technology
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Fan Cao
Hunan Institute of Science and Technology
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panliang zhang
Hunan Institute of Science and Technology
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Jian Ou
Hunan Institute of Science and Technology
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Kewen Tang
Hunan Institute of Science and Technology
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Abstract

Enzyme immobilization enhances the catalytic activity and stability of the enzyme, and also improves reusability. Metal organic frameworks (MOFs), which possess diversified structures and porosity, have been used as excellent carriers for enzyme immobilization. Pseudomonas fluorescens lipase (PFL) has been successfully immobilized onto MOFs by covalent cross-linking to obtain a series of immobilized lipase (PFL@MOFs). PFL@MOFs are used for catalytic enantioselective hydrolysis of 2-(4-hydroxyphenyl) propionic acid ethyl ester enantiomers (2-HPPAEE) in aqueous medium and transesterification of 4-methoxymandelic acid enantiomers (4-MMA) in organic medium. The experimental results indicated that PFL@Uio-66(Zr) exhibits excellent enzymatic catalysis performances and high enantioselectives. In addition, to increase catalytic activity and reusability, PFL is modified by the polyethylene glycol (PEG) to prepare PEG-modified lipase (PFL-PEG), then PFL-PEG is immobilized onto Uio-66(Zr) to prepare PFL-PEG@Uio-66(Zr), demonstrating better reusability and catalytic activity compared with PFL@Uio-66(Zr).

Peer review status:ACCEPTED

03 Feb 2020Submitted to AIChE Journal
04 Feb 2020Submission Checks Completed
04 Feb 2020Assigned to Editor
06 Feb 2020Reviewer(s) Assigned
13 Mar 2020Editorial Decision: Revise Major
21 May 20201st Revision Received
22 May 2020Submission Checks Completed
22 May 2020Assigned to Editor
23 May 2020Reviewer(s) Assigned
07 Jun 2020Editorial Decision: Accept