Next Article in Journal
Differentiation of Dental Pulp Stem Cells on Gutta-Percha Scaffolds
Next Article in Special Issue
Design and Preparation of Nano-Lignin Peroxidase (NanoLiP) by Protein Block Copolymerization Approach
Previous Article in Journal
The Effect of Lithium Iodide to the Properties of Carboxymethyl κ-Carrageenan/Carboxymethyl Cellulose Polymer Electrolyte and Dye-Sensitized Solar Cell Performance
Previous Article in Special Issue
Enzyme-Catalyzed Synthesis of Water-Soluble Conjugated Poly[2-(3-thienyl)-Ethoxy-4-Butylsulfonate]
Article Menu

Export Article

Open AccessArticle
Polymers 2016, 8(5), 194; doi:10.3390/polym8050194

Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit

Enzyme Research Team, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wakoshi, Saitama 351-0198, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Katja Loos
Received: 26 April 2016 / Revised: 10 May 2016 / Accepted: 11 May 2016 / Published: 13 May 2016
(This article belongs to the Special Issue Enzymatic Polymer Synthesis)
View Full-Text   |   Download PDF [2958 KB, uploaded 13 May 2016]   |  

Abstract

Peptides have the potential to serve as an alternative for petroleum-based polymers to support a sustainable society. However, they lack thermoplasticity, owing to their strong intermolecular interactions. In contrast, nylon is famous for its thermoplasticity and chemical resistance. Here, we synthesized peptides containing a nylon unit to modify their thermal properties by using papain-catalyzed chemoenzymatic polymerization. We used l-glutamic acid alkyl ester as the amino acid monomer and nylon 1, 3, 4, and 6 alkyl esters as the nylon unit. Papain catalyzed the copolymerization of glutamic acid with nylon 3, 4, and 6 alkyl esters, whereas the nylon 1 unit could not be copolymerized. Other proteases used in this study, namely, bromelain, proteinase K, and Candida antarctica lipase (CALB), were not able to copolymerize with any nylon units. The broad substrate specificity of papain enabled the copolymerization of l-glutamic acid with a nylon unit. The peptides with nylon units demonstrated different thermal profiles from that of oligo(l-glutamic acid). Therefore, the resultant peptides with various nylon units are expected to form fewer intermolecular hydrogen bonds, thus altering their thermal properties. This finding is expected to broaden the applications of peptide materials and chemoenzymatic polymerization. View Full-Text
Keywords: chemoenzymatic synthesis; aminolysis; peptide; papain; bromelain; proteinase K; lipase; thermal property; nylon chemoenzymatic synthesis; aminolysis; peptide; papain; bromelain; proteinase K; lipase; thermal property; nylon
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Yazawa, K.; Numata, K. Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit. Polymers 2016, 8, 194.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Polymers EISSN 2073-4360 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top