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(1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei

β-glucosidases have received considerable attention due to their essential role in bioethanol production from lignocellulosic biomass. β-glucosidase can hydrolyse cellobiose in cellulose degradation and its low activity has been considered as one of the main limiting steps in the process. Large-scal...

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Autores principales: Makraki, Eleni, Carneiro, Marta G., Heyam, Alex, Eiso, A. B., Siegal, Gregg, Hubbard, Roderick E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462900/
https://www.ncbi.nlm.nih.gov/pubmed/32562251
http://dx.doi.org/10.1007/s12104-020-09959-2
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author Makraki, Eleni
Carneiro, Marta G.
Heyam, Alex
Eiso, A. B.
Siegal, Gregg
Hubbard, Roderick E.
author_facet Makraki, Eleni
Carneiro, Marta G.
Heyam, Alex
Eiso, A. B.
Siegal, Gregg
Hubbard, Roderick E.
author_sort Makraki, Eleni
collection PubMed
description β-glucosidases have received considerable attention due to their essential role in bioethanol production from lignocellulosic biomass. β-glucosidase can hydrolyse cellobiose in cellulose degradation and its low activity has been considered as one of the main limiting steps in the process. Large-scale conversions of cellulose therefore require high enzyme concentration which increases the cost. β-glucosidases with improved activity and thermostability are therefore of great commercial interest. The fungus Trichoderma reseei expresses thermostable cellulolytic enzymes which have been widely studied as attractive targets for industrial applications. Genetically modified β-glucosidases from Trichoderma reseei have been recently commercialised. We have developed an approach in which screening of low molecular weight molecules (fragments) identifies compounds that increase enzyme activity and are currently characterizing fragment-based activators of TrBgl2. A structural analysis of the 55 kDa apo form of TrBgl2 revealed a classical (α/β)(8)-TIM barrel fold. In the present study we present a partial assignment of backbone chemical shifts, along with those of the Ile (I)-Val (V)-Leu (L) methyl groups of TrBgl2. These data will be used to characterize the interaction of TrBgl2 with the small molecule activators.
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spelling pubmed-74629002020-09-11 (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei Makraki, Eleni Carneiro, Marta G. Heyam, Alex Eiso, A. B. Siegal, Gregg Hubbard, Roderick E. Biomol NMR Assign Article β-glucosidases have received considerable attention due to their essential role in bioethanol production from lignocellulosic biomass. β-glucosidase can hydrolyse cellobiose in cellulose degradation and its low activity has been considered as one of the main limiting steps in the process. Large-scale conversions of cellulose therefore require high enzyme concentration which increases the cost. β-glucosidases with improved activity and thermostability are therefore of great commercial interest. The fungus Trichoderma reseei expresses thermostable cellulolytic enzymes which have been widely studied as attractive targets for industrial applications. Genetically modified β-glucosidases from Trichoderma reseei have been recently commercialised. We have developed an approach in which screening of low molecular weight molecules (fragments) identifies compounds that increase enzyme activity and are currently characterizing fragment-based activators of TrBgl2. A structural analysis of the 55 kDa apo form of TrBgl2 revealed a classical (α/β)(8)-TIM barrel fold. In the present study we present a partial assignment of backbone chemical shifts, along with those of the Ile (I)-Val (V)-Leu (L) methyl groups of TrBgl2. These data will be used to characterize the interaction of TrBgl2 with the small molecule activators. Springer Netherlands 2020-06-19 2020 /pmc/articles/PMC7462900/ /pubmed/32562251 http://dx.doi.org/10.1007/s12104-020-09959-2 Text en © The Author(s) 2020 Open AccessThis 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
Makraki, Eleni
Carneiro, Marta G.
Heyam, Alex
Eiso, A. B.
Siegal, Gregg
Hubbard, Roderick E.
(1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title_full (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title_fullStr (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title_full_unstemmed (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title_short (1)H, (13)C, (15)N backbone and IVL methyl group resonance assignment of the fungal β-glucosidase from Trichoderma reesei
title_sort (1)h, (13)c, (15)n backbone and ivl methyl group resonance assignment of the fungal β-glucosidase from trichoderma reesei
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462900/
https://www.ncbi.nlm.nih.gov/pubmed/32562251
http://dx.doi.org/10.1007/s12104-020-09959-2
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