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Catalysts 2019, 9(3), 237; https://doi.org/10.3390/catal9030237

Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine

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College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, China
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State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing 211816, China
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Department of Chemical Engineering, Tsinghua University, Beijing 100084, China
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National Engineering Research Center for Coatings, CNOOC Changzhou Paint and Coatings Industry Research Institute Co., Ltd, Changzhou 213016, China
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Author to whom correspondence should be addressed.
Received: 21 January 2019 / Revised: 27 February 2019 / Accepted: 27 February 2019 / Published: 4 March 2019
(This article belongs to the Special Issue Biocatalysts: Design and Application)
Full-Text   |   PDF [3370 KB, uploaded 4 March 2019]   |  

Abstract

Microenvironment modification within nanoconfinement can maximize the catalytic activity of enzymes. Phospholipase A1 (PLA1) has been used as the biocatalyst to produce high value L-α-glycerylphosphorylcholine (L-α-GPC) through hydrolysis of phosphatidylcholine (PC). We successfully developed a simple co-precipitation method to encapsulate PLA1 in a metal–surfactant nanocomposite (MSNC), then modified it using alkalescent 2-Methylimidazole (2-Melm) to promote catalytic efficiency in biphasic systems. The generated [email protected]1/MSNC showed higher catalytic activity than PLA1/MSNC and free PLA1. Scanning electron microscopy and transmission electron microscopy showed a typical spherical structure of [email protected]1/MSNC at about 50 nm, which was smaller than that of [email protected] Energy disperse spectroscopy, N2 adsorption isotherms, Fourier transform infrared spectrum, and high-resolution X-ray photoelectron spectroscopy proved that 2-Melm successfully modified PLA1/MSNC. The generated [email protected]1/MSNC showed a high catalytic rate per unit enzyme mass of 1.58 μmol mg-1 min-1 for the formation of L-α-GPC. The [email protected]1/MSNC also showed high thermal stability, pH stability, and reusability in a water–hexane biphasic system. The integration of alkaline and amphiphilic properties of a nanocomposite encapsulating PLA1 resulted in highly efficient sequenced reactions of acyl migration and enzymatic hydrolysis at the interface of a biphasic system, which cannot be achieved by free enzyme. View Full-Text
Keywords: metal–surfactant nanocomposite; phospholipase A1; microenvironment modification metal–surfactant nanocomposite; phospholipase A1; microenvironment modification
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Li, H.; Cao, X.; Lu, Y.; Ni, Y.; Wang, X.; Lu, Q.; Li, G.; Chen, K.; Ouyang, P.; Tan, W. Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine. Catalysts 2019, 9, 237.

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