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Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design

The need for cost-effectively produced and improved biocatalysts for industrial, pharmaceutical and environmental processes is steadily increasing. While enzyme properties themselves can be improved via protein engineering, immobilization by attachment to carrier materials remains a critical step fo...

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Detalles Bibliográficos
Autores principales: Rehm, Fabian B. H., Chen, Shuxiong, Rehm, Bernd H. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972917/
https://www.ncbi.nlm.nih.gov/pubmed/28463573
http://dx.doi.org/10.1080/21655979.2017.1325040
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author Rehm, Fabian B. H.
Chen, Shuxiong
Rehm, Bernd H. A.
author_facet Rehm, Fabian B. H.
Chen, Shuxiong
Rehm, Bernd H. A.
author_sort Rehm, Fabian B. H.
collection PubMed
description The need for cost-effectively produced and improved biocatalysts for industrial, pharmaceutical and environmental processes is steadily increasing. While enzyme properties themselves can be improved via protein engineering, immobilization by attachment to carrier materials remains a critical step for stabilization and process implementation. A new emerging immobilization approach, the in situ immobilization, enables simultaneous production of highly active enzymes and carrier materials using bioengineering/synthetic biology of microbial cells. In situ enzyme immobilization holds the promise of cost-effective production of highly functional immobilized biocatalysts for uses such as in bioremediation, drug synthesis, bioenergy and food processing.
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spelling pubmed-59729172018-05-31 Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design Rehm, Fabian B. H. Chen, Shuxiong Rehm, Bernd H. A. Bioengineered Commentary The need for cost-effectively produced and improved biocatalysts for industrial, pharmaceutical and environmental processes is steadily increasing. While enzyme properties themselves can be improved via protein engineering, immobilization by attachment to carrier materials remains a critical step for stabilization and process implementation. A new emerging immobilization approach, the in situ immobilization, enables simultaneous production of highly active enzymes and carrier materials using bioengineering/synthetic biology of microbial cells. In situ enzyme immobilization holds the promise of cost-effective production of highly functional immobilized biocatalysts for uses such as in bioremediation, drug synthesis, bioenergy and food processing. Taylor & Francis 2017-05-19 /pmc/articles/PMC5972917/ /pubmed/28463573 http://dx.doi.org/10.1080/21655979.2017.1325040 Text en © 2018 The Author(s). Published with license by Taylor & Francis http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Rehm, Fabian B. H.
Chen, Shuxiong
Rehm, Bernd H. A.
Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title_full Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title_fullStr Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title_full_unstemmed Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title_short Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design
title_sort bioengineering toward direct production of immobilized enzymes: a paradigm shift in biocatalyst design
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972917/
https://www.ncbi.nlm.nih.gov/pubmed/28463573
http://dx.doi.org/10.1080/21655979.2017.1325040
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