Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit
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 synthe...
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| Format: | Article |
| Language: | English |
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MDPI AG
2016-05-01
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| Series: | Polymers |
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| Online Access: | http://www.mdpi.com/2073-4360/8/5/194 |
| _version_ | 1811263594650664960 |
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| author | Kenjiro Yazawa Keiji Numata |
| author_facet | Kenjiro Yazawa Keiji Numata |
| author_sort | Kenjiro Yazawa |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T19:48:11Z |
| format | Article |
| id | doaj.art-f25ae58a3d5f432cba230c3a28e5b626 |
| institution | Directory Open Access Journal |
| issn | 2073-4360 |
| language | English |
| last_indexed | 2024-04-12T19:48:11Z |
| publishDate | 2016-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Polymers |
| spelling | doaj.art-f25ae58a3d5f432cba230c3a28e5b6262022-12-22T03:18:54ZengMDPI AGPolymers2073-43602016-05-018519410.3390/polym8050194polym8050194Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer UnitKenjiro Yazawa0Keiji Numata1Enzyme Research Team, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wakoshi, Saitama 351-0198, JapanEnzyme Research Team, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wakoshi, Saitama 351-0198, JapanPeptides 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.http://www.mdpi.com/2073-4360/8/5/194chemoenzymatic synthesisaminolysispeptidepapainbromelainproteinase Klipasethermal propertynylon |
| spellingShingle | Kenjiro Yazawa Keiji Numata Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit Polymers chemoenzymatic synthesis aminolysis peptide papain bromelain proteinase K lipase thermal property nylon |
| title | Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit |
| title_full | Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit |
| title_fullStr | Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit |
| title_full_unstemmed | Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit |
| title_short | Papain-Catalyzed Synthesis of Polyglutamate Containing a Nylon Monomer Unit |
| title_sort | papain catalyzed synthesis of polyglutamate containing a nylon monomer unit |
| topic | chemoenzymatic synthesis aminolysis peptide papain bromelain proteinase K lipase thermal property nylon |
| url | http://www.mdpi.com/2073-4360/8/5/194 |
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