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Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization
The utilization of scaffolds for enzyme immobilization involves advanced bionanotechnology applications in biorefinery fields, which can be achieved by optimizing the function of various enzymes. This review presents various current scaffolding techniques based on proteins, microbes and nanomaterial...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
WILEY‐VCH Verlag
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5132044/ https://www.ncbi.nlm.nih.gov/pubmed/27783468 http://dx.doi.org/10.1002/biot.201600039 |
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author | Hyeon, Jeong Eun Shin, Sang Kyu Han, Sung Ok |
author_facet | Hyeon, Jeong Eun Shin, Sang Kyu Han, Sung Ok |
author_sort | Hyeon, Jeong Eun |
collection | PubMed |
description | The utilization of scaffolds for enzyme immobilization involves advanced bionanotechnology applications in biorefinery fields, which can be achieved by optimizing the function of various enzymes. This review presents various current scaffolding techniques based on proteins, microbes and nanomaterials for enzyme immobilization, as well as the impact of these techniques on the biorefinery of lignocellulosic materials. Among them, architectural scaffolds have applied to useful strategies for protein engineering to improve the performance of immobilized enzymes in several industrial and research fields. In complexed enzyme systems that have critical roles in carbon metabolism, scaffolding proteins assemble different proteins in relatively durable configurations and facilitate collaborative protein interactions and functions. Additionally, a microbial strain, combined with designer enzyme complexes, can be applied to the immobilizing scaffold because the in vivo immobilizing technique has several benefits in enzymatic reaction systems related to both synthetic biology and metabolic engineering. Furthermore, with the advent of nanotechnology, nanomaterials possessing ideal physicochemical characteristics, such as mass transfer resistance, specific surface area and efficient enzyme loading, can be applied as novel and interesting scaffolds for enzyme immobilization. Intelligent application of various scaffolds to couple with nanoscale engineering tools and metabolic engineering technology may offer particular benefits in research. |
format | Online Article Text |
id | pubmed-5132044 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | WILEY‐VCH Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-51320442016-12-02 Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization Hyeon, Jeong Eun Shin, Sang Kyu Han, Sung Ok Biotechnol J Reviews The utilization of scaffolds for enzyme immobilization involves advanced bionanotechnology applications in biorefinery fields, which can be achieved by optimizing the function of various enzymes. This review presents various current scaffolding techniques based on proteins, microbes and nanomaterials for enzyme immobilization, as well as the impact of these techniques on the biorefinery of lignocellulosic materials. Among them, architectural scaffolds have applied to useful strategies for protein engineering to improve the performance of immobilized enzymes in several industrial and research fields. In complexed enzyme systems that have critical roles in carbon metabolism, scaffolding proteins assemble different proteins in relatively durable configurations and facilitate collaborative protein interactions and functions. Additionally, a microbial strain, combined with designer enzyme complexes, can be applied to the immobilizing scaffold because the in vivo immobilizing technique has several benefits in enzymatic reaction systems related to both synthetic biology and metabolic engineering. Furthermore, with the advent of nanotechnology, nanomaterials possessing ideal physicochemical characteristics, such as mass transfer resistance, specific surface area and efficient enzyme loading, can be applied as novel and interesting scaffolds for enzyme immobilization. Intelligent application of various scaffolds to couple with nanoscale engineering tools and metabolic engineering technology may offer particular benefits in research. WILEY‐VCH Verlag 2016-10-26 2016-11 /pmc/articles/PMC5132044/ /pubmed/27783468 http://dx.doi.org/10.1002/biot.201600039 Text en © 2016 The Authors. Biotechnology Journal published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs (http://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Reviews Hyeon, Jeong Eun Shin, Sang Kyu Han, Sung Ok Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title | Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title_full | Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title_fullStr | Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title_full_unstemmed | Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title_short | Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
title_sort | design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5132044/ https://www.ncbi.nlm.nih.gov/pubmed/27783468 http://dx.doi.org/10.1002/biot.201600039 |
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