Immobilization of Penicillin G Acylase on Magnetic Nanoparticles Modified by Ionic Liquids
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2021, Ionic Liquid-Based Technologies for Environmental SustainabilityAn enzyme-loaded reactor using metal-organic framework-templated polydopamine microcapsule
2021, Chinese Journal of Chemical EngineeringCitation Excerpt :While enzymatic catalysis has many important advantages compared with chemical catalysis, such as high specificity, high selectivity, and mild operational conditions, the use of free enzymes for industrial applications still features several inherent limitations including low operational stability and the difficulties of recovery and recycling. Immobilization of enzymes on solid carriers can conquer these limitations by providing improved enzyme stability and high reusability [1–17]. As a result, the exploration and development of new and efficient solid supports are highly desirable to create immobilized enzymes with enhanced stability and high reusability while retaining its original activity and selectivity.
Metal affinity immobilization of cellulase on Fe <inf>3</inf> O <inf>4</inf> nanoparticles with copper as ligand for biocatalytic applications
2019, Food ChemistryCitation Excerpt :The saturation magnetization values of MNPs-APTES and MNPs-APTES-Cu were 56.3 and 23.3 emu/g, respectively, which were less than that of Fe3O4 nanoparticles, due to the existence of different shells. Furthermore, there was no hysteresis in the magnetization curve and no remnant magnetization was observed for all of the samples, which implied their superparamagnetism behaviour (Zhou et al., 2012). Fig. 2A shows a fairly low loading of copper on nanoparticles in the absence of buffer (with deionized water at pH = 8) compared with high copper loading in the presence of sodium phosphate buffer at pH = 8.
Covalent immobilization and characterization of penicillin G acylase on amino and GO functionalized magnetic Ni<inf>0.5</inf>Zn<inf>0.5</inf>Fe<inf>2</inf>O<inf>4</inf>@SiO<inf>2</inf> nanocomposite prepared via a novel rapid-combustion process
2019, International Journal of Biological Macromolecules
Supported by the National Basic Research Program of China (2007CB613507).