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Environmental biodegradability of recombinant structural protein
Next generation polymers needs to be produced from renewable sources and to be converted into inorganic compounds in the natural environment at the end of life. Recombinant structural protein is a promising alternative to conventional engineering plastics due to its good thermal and mechanical prope...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794409/ https://www.ncbi.nlm.nih.gov/pubmed/33420166 http://dx.doi.org/10.1038/s41598-020-80114-6 |
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author | Tachibana, Yuya Darbe, Sunita Hayashi, Senri Kudasheva, Alina Misawa, Haruna Shibata, Yuka Kasuya, Ken-ichi |
author_facet | Tachibana, Yuya Darbe, Sunita Hayashi, Senri Kudasheva, Alina Misawa, Haruna Shibata, Yuka Kasuya, Ken-ichi |
author_sort | Tachibana, Yuya |
collection | PubMed |
description | Next generation polymers needs to be produced from renewable sources and to be converted into inorganic compounds in the natural environment at the end of life. Recombinant structural protein is a promising alternative to conventional engineering plastics due to its good thermal and mechanical properties, its production from biomass, and its potential for biodegradability. Herein, we measured the thermal and mechanical properties of the recombinant structural protein BP1 and evaluated its biodegradability. Because the thermal degradation occurs above 250 °C and the glass transition temperature is 185 °C, BP1 can be molded into sheets by a manual hot press at 150 °C and 83 MPa. The flexural strength and modulus of BP1 were 115 ± 6 MPa and 7.38 ± 0.03 GPa. These properties are superior to those of commercially available biodegradable polymers. The biodegradability of BP1 was carefully evaluated. BP1 was shown to be efficiently hydrolyzed by some isolated bacterial strains in a dispersed state. Furthermore, it was readily hydrolyzed from the solid state by three isolated proteases. The mineralization was evaluated by the biochemical oxygen demand (BOD)-biodegradation testing with soil inocula. The BOD biodegradability of BP1 was 70.2 ± 6.0 after 33 days. |
format | Online Article Text |
id | pubmed-7794409 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-77944092021-01-11 Environmental biodegradability of recombinant structural protein Tachibana, Yuya Darbe, Sunita Hayashi, Senri Kudasheva, Alina Misawa, Haruna Shibata, Yuka Kasuya, Ken-ichi Sci Rep Article Next generation polymers needs to be produced from renewable sources and to be converted into inorganic compounds in the natural environment at the end of life. Recombinant structural protein is a promising alternative to conventional engineering plastics due to its good thermal and mechanical properties, its production from biomass, and its potential for biodegradability. Herein, we measured the thermal and mechanical properties of the recombinant structural protein BP1 and evaluated its biodegradability. Because the thermal degradation occurs above 250 °C and the glass transition temperature is 185 °C, BP1 can be molded into sheets by a manual hot press at 150 °C and 83 MPa. The flexural strength and modulus of BP1 were 115 ± 6 MPa and 7.38 ± 0.03 GPa. These properties are superior to those of commercially available biodegradable polymers. The biodegradability of BP1 was carefully evaluated. BP1 was shown to be efficiently hydrolyzed by some isolated bacterial strains in a dispersed state. Furthermore, it was readily hydrolyzed from the solid state by three isolated proteases. The mineralization was evaluated by the biochemical oxygen demand (BOD)-biodegradation testing with soil inocula. The BOD biodegradability of BP1 was 70.2 ± 6.0 after 33 days. Nature Publishing Group UK 2021-01-08 /pmc/articles/PMC7794409/ /pubmed/33420166 http://dx.doi.org/10.1038/s41598-020-80114-6 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Tachibana, Yuya Darbe, Sunita Hayashi, Senri Kudasheva, Alina Misawa, Haruna Shibata, Yuka Kasuya, Ken-ichi Environmental biodegradability of recombinant structural protein |
title | Environmental biodegradability of recombinant structural protein |
title_full | Environmental biodegradability of recombinant structural protein |
title_fullStr | Environmental biodegradability of recombinant structural protein |
title_full_unstemmed | Environmental biodegradability of recombinant structural protein |
title_short | Environmental biodegradability of recombinant structural protein |
title_sort | environmental biodegradability of recombinant structural protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794409/ https://www.ncbi.nlm.nih.gov/pubmed/33420166 http://dx.doi.org/10.1038/s41598-020-80114-6 |
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