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Catalysts 2018, 8(9), 401; https://doi.org/10.3390/catal8090401

Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance

1
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China
2
Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, China
*
Authors to whom correspondence should be addressed.
Received: 7 September 2018 / Revised: 16 September 2018 / Accepted: 17 September 2018 / Published: 18 September 2018
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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Abstract

In this study, chitosanase cloning from Streptomyces albolongus was fermented and purified by a Ni-NTA column. Fe3O4-SiO2 magnetite nanoparticles (MNPs) were synthesized by the co-precipitation method coating with silica via a sol-gel reaction and were then amino functioned by treating with 3-aminopropyltriethoxysilane. Chitosanases were immobilized onto the surface of MNPs by covalent bonding ([email protected]). Transmission electron microscopy (TEM), Fourier transform infrared spectrometer (FT–IR), and magnetic measurements were used to illustrate the MNPs and immobilized chitosanase. The optimal conditions of immobilization were studied. The thermal, pH, and stabilities of immobilized chitosanase were tested and the results showed that the stabilities were significantly enhanced compared with free chitosanase. After being recycled 10 times, the residual activity of the immobilized chitosanase was 43.7% of the initial activity. View Full-Text
Keywords: chitosanase; enzyme immobilization; magnetic nanoparticles; covalent bonding chitosanase; enzyme immobilization; magnetic nanoparticles; covalent bonding
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Wang, W.; Guo, N.; Huang, W.; Zhang, Z.; Mao, X. Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance. Catalysts 2018, 8, 401.

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