Journal
CATALYSTS
Volume 7, Issue 2, Pages -Publisher
MDPI AG
DOI: 10.3390/catal7020049
Keywords
lipase; immobilization; polydopamine; Fe3O4 nanoparticle; core-shell structure; ester hydrolysis; kinetic resolution
Categories
Funding
- Natural Science Foundation of China [81373344, 51403074]
- Science & Technology Department of Jilin Province [20140101140JC, 20160520144JH, 20160520146JH]
- Education Department of Jilin Province [2015469]
- Youth Fund of Health and Family Planning Commission of Jilin Province [2013Q026]
- Norman Bethune Program of Jilin University [2015324, 2015423]
- Graduate Innovation Program of Jilin University [2016149]
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Here, core-shell structured polydopamine-coated Fe3O4 nanoparticles were constructed to immobilize thermostable lipase QLM from Alcaligenes sp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 +/- 1.47 mg/g immobilized enzyme. Then, the immobilized enzyme was demonstrated to possess favorable catalytic activity and stability in the ester hydrolysis, using p-nitrophenyl caprylate as the substrate. Further, it was successfully employed in the kinetic resolution of (R, S)-2-octanol, and satisfactory enantioselectivity and recyclability could be obtained with an enantiomeric ratio (E) of 8-15 over 10 cycle reactions. Thus, core-shell structured polydopamine-coated Fe3O4 nanoparticles can be potentially used as a carrier for enzyme immobilization to improve their activity, stability, and reusability, which is beneficial for constructing efficient catalysts for industrial biocatalysis.
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