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Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges

[Image: see text] The constant rise in energy demands, costs, and concerns about global warming has created a demand for new renewable alternative fuels that can be produced sustainably. Lignocellulose biomass can act as an excellent energy source and various value-added compounds like xylitol. In t...

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Autores principales: Ali, Nabeel, Aiman, Ayesha, Shamsi, Anas, Hassan, Imtaiyaz, Shahid, Mohammad, Gaur, Naseem A., Islam, Asimul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9730754/
https://www.ncbi.nlm.nih.gov/pubmed/36506193
http://dx.doi.org/10.1021/acsomega.2c05690
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author Ali, Nabeel
Aiman, Ayesha
Shamsi, Anas
Hassan, Imtaiyaz
Shahid, Mohammad
Gaur, Naseem A.
Islam, Asimul
author_facet Ali, Nabeel
Aiman, Ayesha
Shamsi, Anas
Hassan, Imtaiyaz
Shahid, Mohammad
Gaur, Naseem A.
Islam, Asimul
author_sort Ali, Nabeel
collection PubMed
description [Image: see text] The constant rise in energy demands, costs, and concerns about global warming has created a demand for new renewable alternative fuels that can be produced sustainably. Lignocellulose biomass can act as an excellent energy source and various value-added compounds like xylitol. In this research study, we have explored the xylose reductase that was obtained from the genome of a thermophilic fungus Thermothelomyces thermophilus while searching for an enzyme to convert xylose to xylitol at higher temperatures. The recombinant thermostable TtXR histidine-tagged fusion protein was expressed in Escherichia coli and successfully purified for the first time. Further, it was characterized for its function and novel structure at varying temperatures and pH. The enzyme showed maximal activity at 7.0 pH and favored  d-xylose over other pentoses and hexoses. Biophysical approaches such as ultraviolet–visible (UV–visible), fluorescence spectrometry, and far-UV circular dichroism (CD) spectroscopy were used to investigate the structural integrity of pure TtXR. This research highlights the potential application of uncharacterized xylose reductase as an alternate source for the effective utilization of lignocellulose in fermentation industries at elevated temperatures. Moreover, this research would give environment-friendly and long-term value-added products, like xylitol, from lignocellulosic feedstock for both scientific and commercial purposes.
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spelling pubmed-97307542022-12-09 Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges Ali, Nabeel Aiman, Ayesha Shamsi, Anas Hassan, Imtaiyaz Shahid, Mohammad Gaur, Naseem A. Islam, Asimul ACS Omega [Image: see text] The constant rise in energy demands, costs, and concerns about global warming has created a demand for new renewable alternative fuels that can be produced sustainably. Lignocellulose biomass can act as an excellent energy source and various value-added compounds like xylitol. In this research study, we have explored the xylose reductase that was obtained from the genome of a thermophilic fungus Thermothelomyces thermophilus while searching for an enzyme to convert xylose to xylitol at higher temperatures. The recombinant thermostable TtXR histidine-tagged fusion protein was expressed in Escherichia coli and successfully purified for the first time. Further, it was characterized for its function and novel structure at varying temperatures and pH. The enzyme showed maximal activity at 7.0 pH and favored  d-xylose over other pentoses and hexoses. Biophysical approaches such as ultraviolet–visible (UV–visible), fluorescence spectrometry, and far-UV circular dichroism (CD) spectroscopy were used to investigate the structural integrity of pure TtXR. This research highlights the potential application of uncharacterized xylose reductase as an alternate source for the effective utilization of lignocellulose in fermentation industries at elevated temperatures. Moreover, this research would give environment-friendly and long-term value-added products, like xylitol, from lignocellulosic feedstock for both scientific and commercial purposes. American Chemical Society 2022-11-17 /pmc/articles/PMC9730754/ /pubmed/36506193 http://dx.doi.org/10.1021/acsomega.2c05690 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Ali, Nabeel
Aiman, Ayesha
Shamsi, Anas
Hassan, Imtaiyaz
Shahid, Mohammad
Gaur, Naseem A.
Islam, Asimul
Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title_full Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title_fullStr Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title_full_unstemmed Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title_short Identification of Thermostable Xylose Reductase from Thermothelomyces thermophilus: A Biochemical Characterization Approach to Meet Biofuel Challenges
title_sort identification of thermostable xylose reductase from thermothelomyces thermophilus: a biochemical characterization approach to meet biofuel challenges
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9730754/
https://www.ncbi.nlm.nih.gov/pubmed/36506193
http://dx.doi.org/10.1021/acsomega.2c05690
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