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Authors = Xingyi Lyu

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10 pages, 2655 KiB  
Article
Synthesis and Characterization of Mesoporous Silica Nanoparticles Loaded with Pt Catalysts
by Xingyi Lyu, Xun Wu, Yuzi Liu, Wenyu Huang, Byeongdu Lee and Tao Li
Catalysts 2022, 12(2), 183; https://doi.org/10.3390/catal12020183 - 31 Jan 2022
Cited by 15 | Viewed by 5208
Abstract
Coating the catalyst with a nanoporous layer has been demonstrated to be an effective approach to improve catalyst stability. Herein, we systematically investigate two types of core-shell mesoporous silica nanoparticles with a platinum nanocatalyst using a variety of characterization methods. One of the [...] Read more.
Coating the catalyst with a nanoporous layer has been demonstrated to be an effective approach to improve catalyst stability. Herein, we systematically investigate two types of core-shell mesoporous silica nanoparticles with a platinum nanocatalyst using a variety of characterization methods. One of the mesoporous particles has a unique amine ring structure in the middle of a shell (Ring-mSiO2/Pt-5.0/SiO2), and the other one has no ring structure (mSiO2/Pt-5.0/SiO2). Brunauer–Emmett–Teller/Barrett–Joyner–Halenda (BET/BJH) presented a similar surface area for both particles, and the pore size was 2.4 nm. Ultra-Small-Angle X-ray Scattering (USAXS)/ Small-Angle X-ray Scattering (SAXS) showed the size of mSiO2/Pt-5.0/SiO2 and Ring-mSiO2/Pt-5.0/SiO2 were 420 nm and 272 nm, respectively. It also showed that the ring structure was 30 nm above the silica core. Using high-resolution Transmission Electron Microscopy (TEM), it was found that the platinum nanoparticles are loaded evenly on the surface of the silica. In situ SAXS heating experiments and Thermogravimetric Analysis (TGA) indicated that the mSiO2/Pt-5.0/SiO2 were more stable during the high temperature, while the Ring-mSiO2/Pt-5.0/SiO2 had more change in the particle. Full article
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15 pages, 2221 KiB  
Review
Immobilization of Enzymes by Polymeric Materials
by Xingyi Lyu, Rebekah Gonzalez, Andalwisye Horton and Tao Li
Catalysts 2021, 11(10), 1211; https://doi.org/10.3390/catal11101211 - 9 Oct 2021
Cited by 73 | Viewed by 10683
Abstract
Enzymes are the highly efficient biocatalyst in modern biotechnological industries. Due to the fragile property exposed to the external stimulus, the application of enzymes is highly limited. The immobilized enzyme by polymer has become a research hotspot to empower enzymes with more extraordinary [...] Read more.
Enzymes are the highly efficient biocatalyst in modern biotechnological industries. Due to the fragile property exposed to the external stimulus, the application of enzymes is highly limited. The immobilized enzyme by polymer has become a research hotspot to empower enzymes with more extraordinary properties and broader usage. Compared with free enzyme, polymer immobilized enzymes improve thermal and operational stability in harsh environments, such as extreme pH, temperature and concentration. Furthermore, good reusability is also highly expected. The first part of this study reviews the three primary immobilization methods: physical adsorption, covalent binding and entrapment, with their advantages and drawbacks. The second part of this paper includes some polymer applications and their derivatives in the immobilization of enzymes. Full article
(This article belongs to the Special Issue Towards Polymeric Biocatalysts)
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