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Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases
Lignin is a major obstacle for cost-effective conversion of cellulose into fermentable sugars. Non-productive adsorption onto insoluble lignin fragments and interactions with soluble phenols are important inhibition mechanisms of cellulases, including β-glucosidases. Here, we examined the inhibitory...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5519169/ https://www.ncbi.nlm.nih.gov/pubmed/28727856 http://dx.doi.org/10.1371/journal.pone.0181629 |
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author | da Silva, Viviam M. Sato, Juliana A. P. Araujo, Juscemácia N. Squina, Fabio M. Muniz, João R. C. Riske, Karin A. Garcia, Wanius |
author_facet | da Silva, Viviam M. Sato, Juliana A. P. Araujo, Juscemácia N. Squina, Fabio M. Muniz, João R. C. Riske, Karin A. Garcia, Wanius |
author_sort | da Silva, Viviam M. |
collection | PubMed |
description | Lignin is a major obstacle for cost-effective conversion of cellulose into fermentable sugars. Non-productive adsorption onto insoluble lignin fragments and interactions with soluble phenols are important inhibition mechanisms of cellulases, including β-glucosidases. Here, we examined the inhibitory effect of tannic acid (TAN), a model polyphenolic compound, on β-glucosidases from the bacterium Thermotoga petrophila (TpBGL1 and TpBGL3) and archaeon Pyrococcus furiosus (PfBGL1). The results revealed that the inhibition effects on β-glucosidases were TAN concentration-dependent. TpBGL1 and TpBGL3 were more tolerant to the presence of TAN when compared with PfBGL1, while TpBGL1 was less inhibited when compared with TpBGL3. In an attempt to better understand the inhibitory effect, the interaction between TAN and β-glucosidases were analyzed by isothermal titration calorimetry (ITC). Furthermore, the exposed hydrophobic surface areas in β-glucosidases were analyzed using a fluorescent probe and compared with the results of inhibition and ITC. The binding constants determined by ITC for the interactions between TAN and β-glucosidases presented the same order of magnitude. However, the number of binding sites and exposed hydrophobic surface areas varied for the β-glucosidases studied. The binding between TAN and β-glucosidases were driven by enthalpic effects and with an unfavorable negative change in entropy upon binding. Furthermore, the data suggest that there is a high correlation between exposed hydrophobic surface areas and the number of binding sites on the inhibition of microbial β-glucosidases by TAN. These studies can be useful for biotechnological applications. |
format | Online Article Text |
id | pubmed-5519169 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-55191692017-08-07 Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases da Silva, Viviam M. Sato, Juliana A. P. Araujo, Juscemácia N. Squina, Fabio M. Muniz, João R. C. Riske, Karin A. Garcia, Wanius PLoS One Research Article Lignin is a major obstacle for cost-effective conversion of cellulose into fermentable sugars. Non-productive adsorption onto insoluble lignin fragments and interactions with soluble phenols are important inhibition mechanisms of cellulases, including β-glucosidases. Here, we examined the inhibitory effect of tannic acid (TAN), a model polyphenolic compound, on β-glucosidases from the bacterium Thermotoga petrophila (TpBGL1 and TpBGL3) and archaeon Pyrococcus furiosus (PfBGL1). The results revealed that the inhibition effects on β-glucosidases were TAN concentration-dependent. TpBGL1 and TpBGL3 were more tolerant to the presence of TAN when compared with PfBGL1, while TpBGL1 was less inhibited when compared with TpBGL3. In an attempt to better understand the inhibitory effect, the interaction between TAN and β-glucosidases were analyzed by isothermal titration calorimetry (ITC). Furthermore, the exposed hydrophobic surface areas in β-glucosidases were analyzed using a fluorescent probe and compared with the results of inhibition and ITC. The binding constants determined by ITC for the interactions between TAN and β-glucosidases presented the same order of magnitude. However, the number of binding sites and exposed hydrophobic surface areas varied for the β-glucosidases studied. The binding between TAN and β-glucosidases were driven by enthalpic effects and with an unfavorable negative change in entropy upon binding. Furthermore, the data suggest that there is a high correlation between exposed hydrophobic surface areas and the number of binding sites on the inhibition of microbial β-glucosidases by TAN. These studies can be useful for biotechnological applications. Public Library of Science 2017-07-20 /pmc/articles/PMC5519169/ /pubmed/28727856 http://dx.doi.org/10.1371/journal.pone.0181629 Text en © 2017 da Silva et al 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 author and source are credited. |
spellingShingle | Research Article da Silva, Viviam M. Sato, Juliana A. P. Araujo, Juscemácia N. Squina, Fabio M. Muniz, João R. C. Riske, Karin A. Garcia, Wanius Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title | Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title_full | Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title_fullStr | Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title_full_unstemmed | Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title_short | Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
title_sort | systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5519169/ https://www.ncbi.nlm.nih.gov/pubmed/28727856 http://dx.doi.org/10.1371/journal.pone.0181629 |
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