Recombinant Protein Polymers

A special issue of Polymers (ISSN 2073-4360). This special issue belongs to the section "Biomacromolecules, Biobased and Biodegradable Polymers".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 2345

Special Issue Editor

Department of Chemical Engineering and Biotechnology, National Taipei University of Technology (Taipei Tech), Taipei 10608, Taiwan
Interests: Protein structure and function, AFM single molecule forces, biomimetic adhesives, protein hydrogels, wound adhesive dressings

Special Issue Information

Dear Colleagues,

Genetic engineering has significant impacts globally, which has enabled the synthesis of protein-based polymers and changed the philosophy of pharmacology, medicine, and industry. Recombinant protein polymers are long-chain molecules of repetitive amino acid motifs that mimic natural structural proteins. The precise control of molecular architecture at high yield creates the possibility of genetically engineered polymers for high-performance materials applications. For example, incorporated motifs at specified locations by recombinant techniques allow protein polymers with tunable functionalities, including sensitivity to environmental stimuli, complexation with drugs, and desired recognition with other molecules. Accordingly, this Special Issue aims to cover the design, synthesis, characterization, manufacturing, and modeling of recombinant protein polymers for controlled drug and gene delivery, tissue engineering, and other biomedical applications, as well as improvements for specific industrial applications.

Prof. Dr. Yang Wei
Guest Editor

Manuscript Submission Information

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Keywords

  • natural building blocks
  • commercialization
  • biomimetic materials
  • recombinant technology
  • protein polymers

Published Papers (1 paper)

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Research

11 pages, 2432 KiB  
Article
Entrapment of the Fastest Known Carbonic Anhydrase with Biomimetic Silica and Its Application for CO2 Sequestration
by Chia-Jung Hsieh, Ju-Chuan Cheng, Chia-Jung Hu and Chi-Yang Yu
Polymers 2021, 13(15), 2452; https://0-doi-org.brum.beds.ac.uk/10.3390/polym13152452 - 26 Jul 2021
Cited by 7 | Viewed by 1922
Abstract
Capturing and storing CO2 is of prime importance. The rate of CO2 sequestration is often limited by the hydration of CO2, which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to [...] Read more.
Capturing and storing CO2 is of prime importance. The rate of CO2 sequestration is often limited by the hydration of CO2, which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to improve the stability and reusability of CA, a silica-condensing peptide (R5) was fused with the fastest known CA from Sulfurihydrogenibium azorense (SazCA) to form R5-SazCA; the fusion protein successfully performed in vitro silicification. The entrapment efficiency reached 100% and the silicified form (R5-SazCA-SP) showed a high activity recovery of 91%. The residual activity of R5-SazCA-SP was two-fold higher than that of the free form when stored at 25 °C for 35 days; R5-SazCA-SP still retained 86% of its activity after 10 cycles of reuse. Comparing with an uncatalyzed reaction, the time required for the onset of CaCO3 formation was shortened by 43% and 33% with the addition of R5-SazCA and R5-SazCA-SP, respectively. R5-SazCA-SP shows great potential as a robust and efficient biocatalyst for CO2 sequestration because of its high activity, high stability, and reusability. Full article
(This article belongs to the Special Issue Recombinant Protein Polymers)
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