Next Article in Journal
Aqueous Phase Hydrogenolysis of Bio-Derivable Furfuryl Alcohol to Pentanediols Using Copper Catalysts
Next Article in Special Issue
Stabilization of a Lipolytic Enzyme for Commercial Application
Previous Article in Journal
Morphology-Dependent Properties of Cu/CeO2 Catalysts for the Water-Gas Shift Reaction
Previous Article in Special Issue
Sucrose Hydrolysis in a Bespoke Capillary Wall-Coated Microreactor
Open AccessArticle

Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

1
Department of Urology, First Hospital of Jilin University, Changchun 130012, China
2
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China
3
Innovative Drug Research Centre, School of Pharmacy, Chongqing University, Chongqing 401331, China
*
Authors to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Catalysts 2017, 7(2), 49; https://doi.org/10.3390/catal7020049
Received: 9 December 2016 / Revised: 18 January 2017 / Accepted: 25 January 2017 / Published: 6 February 2017
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
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. View Full-Text
Keywords: lipase; immobilization; polydopamine; Fe3O4 nanoparticle; core-shell structure; ester hydrolysis; kinetic resolution lipase; immobilization; polydopamine; Fe3O4 nanoparticle; core-shell structure; ester hydrolysis; kinetic resolution
Show Figures

Figure 1

MDPI and ACS Style

Wang, C.; Han, H.; Jiang, W.; Ding, X.; Li, Q.; Wang, Y. Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles. Catalysts 2017, 7, 49.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map

1
Back to TopTop