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Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review
β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stabili...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343665/ https://www.ncbi.nlm.nih.gov/pubmed/37446652 http://dx.doi.org/10.3390/molecules28134990 |
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author | Ouyang, Bei Wang, Guoping Zhang, Nian Zuo, Jiali Huang, Yunhong Zhao, Xihua |
author_facet | Ouyang, Bei Wang, Guoping Zhang, Nian Zuo, Jiali Huang, Yunhong Zhao, Xihua |
author_sort | Ouyang, Bei |
collection | PubMed |
description | β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering. |
format | Online Article Text |
id | pubmed-10343665 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103436652023-07-14 Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review Ouyang, Bei Wang, Guoping Zhang, Nian Zuo, Jiali Huang, Yunhong Zhao, Xihua Molecules Review β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering. MDPI 2023-06-25 /pmc/articles/PMC10343665/ /pubmed/37446652 http://dx.doi.org/10.3390/molecules28134990 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Ouyang, Bei Wang, Guoping Zhang, Nian Zuo, Jiali Huang, Yunhong Zhao, Xihua Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title | Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title_full | Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title_fullStr | Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title_full_unstemmed | Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title_short | Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review |
title_sort | recent advances in β-glucosidase sequence and structure engineering: a brief review |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343665/ https://www.ncbi.nlm.nih.gov/pubmed/37446652 http://dx.doi.org/10.3390/molecules28134990 |
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