Towards Polymeric Biocatalysts

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (28 February 2022) | Viewed by 11279

Special Issue Editors


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Guest Editor
1. Department of Chemistry and Biochemistry, Northern Illinois University, 1425 W Lincoln Hwy, DeKalb, IL 60115, USA
2. X-ray Science Division, Argonne National Laboratory, 9700 S. Cass Ave, Lemont, IL 60439, USA
Interests: medical; energy; protein; catalyst; battery; electrolyte; self-assembly; synchrotron X-ray technique; SAXS; XAS; single-atom catalyst; ALD

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Guest Editor
Centre for Cell Factories and Biopolymers, Griffith Institute for Drug Discovery, Griffith University (Nathan Campus), Brisbane, QLD 4111, Australia
Interests: bionanotechnology; nanoparticles; particulate vaccines; industrial biotechnological diagnostics; biosensor; bioseparation; biocatalyst

Special Issue Information

Dear Colleagues,

Enzymes are the most effective biocatalysts approved by nature, which can achieve faster reactions and higher energy efficiency. Unlike other conventional chemical catalysts, biocatalysts are biodegradable and have high selectivity in water under mild conditions. Enzymes have been widely used to convert chemicals to make useful fuels and medicines, kill diseases, detoxify nerve agents, and treat environmental pollution. Recently, it has attracted significant interest in plastic recycling. However, enzymes cannot always economically compete with traditional chemical and inorganic catalysts. The main challenges preventing the widespread use of enzymatic biocatalysts are high cost, limited stability, and separation difficulties. For commercial-scale processes, enzymes are usually immobilized on solid supports for reuse or recycling. If done effectively, immobilization may be advantageous. Among all the methods available, the method of stabilizing enzymes with polymers or polymer-derived particles as support has many advantages in medical and energy applications. Current methods of forming such structures involve direct conjugation or self-assembly, adsorption, microfluidic synthesis, and electrostatic assembly.

This Special Issue aims to demonstrate the latest developments and trends in biocatalyst design and characterization through controlled assembly or synthesis with polymers or other nanostructures.

Prof. Dr. Tao Li
Dr. Shuxiong Chen
Guest Editor

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Keywords

  • Polymer
  • immobilization
  • self-assembly
  • biocatalyst
  • enzyme
  • functionality
  • adsorption
  • nanoparticle

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Published Papers (2 papers)

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Research

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8 pages, 1465 KiB  
Article
Synthesis and Advanced Characterization of Polymer–Protein Core–Shell Nanoparticles
by Erik Sarnello and Tao Li
Catalysts 2021, 11(6), 730; https://doi.org/10.3390/catal11060730 - 13 Jun 2021
Cited by 2 | Viewed by 2294
Abstract
Enzyme immobilization techniques are widely researched due to their wide range of applications. Polymer–protein core–shell nanoparticles (CSNPs) have emerged as a promising technique for enzyme/protein immobilization via a self-assembly process. Based on the desired application, different sizes and distribution of the polymer–protein CSNPs [...] Read more.
Enzyme immobilization techniques are widely researched due to their wide range of applications. Polymer–protein core–shell nanoparticles (CSNPs) have emerged as a promising technique for enzyme/protein immobilization via a self-assembly process. Based on the desired application, different sizes and distribution of the polymer–protein CSNPs may be required. This work systematically studies the assembly process of poly(4-vinyl pyridine) and bovine serum albumin CSNPs. Average particle size was controlled by varying the concentrations of each reagent. Particle size and size distributions were monitored by dynamic light scattering, ultra-small-angle X-ray scattering, small-angle X-ray scattering and transmission electron microscopy. Results showed a wide range of CSNPs could be assembled ranging from an average radius as small as 52.3 nm, to particles above 1 µm by adjusting reagent concentrations. In situ X-ray scattering techniques monitored particle assembly as a function of time showing the initial particle growth followed by a decrease in particle size as they reach equilibrium. The results outline a general strategy that can be applied to other CSNP systems to better control particle size and distribution for various applications. Full article
(This article belongs to the Special Issue Towards Polymeric Biocatalysts)
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Review

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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 51 | Viewed by 8123
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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