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Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically
Studies have reported that flavonoids inhibit xanthine oxidase (XO) activity; however, poor solubility and stability in lipophilic media limit their bioavailability and applications. This study evaluated the kinetic parameters of XO inhibition and partition coefficients of flavonoid esters biosynthe...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6445226/ https://www.ncbi.nlm.nih.gov/pubmed/28718686 http://dx.doi.org/10.1080/14756366.2017.1347165 |
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author | de Araújo, Maria Elisa Melo Branco Franco, Yollanda Edwirges Moreira Alberto, Thiago Grando Messias, Marcia Cristina Fernandes Leme, Camila Wielewski Sawaya, Alexandra Christine Helena Frankland Carvalho, Patricia de Oliveira |
author_facet | de Araújo, Maria Elisa Melo Branco Franco, Yollanda Edwirges Moreira Alberto, Thiago Grando Messias, Marcia Cristina Fernandes Leme, Camila Wielewski Sawaya, Alexandra Christine Helena Frankland Carvalho, Patricia de Oliveira |
author_sort | de Araújo, Maria Elisa Melo Branco |
collection | PubMed |
description | Studies have reported that flavonoids inhibit xanthine oxidase (XO) activity; however, poor solubility and stability in lipophilic media limit their bioavailability and applications. This study evaluated the kinetic parameters of XO inhibition and partition coefficients of flavonoid esters biosynthesised from hesperidin, naringin, and rutin via enzymatic acylation with hexanoic, octanoic, decanoic, lauric, and oleic acids catalysed by Candida antarctica lipase B (CALB). Quantitative determination by ultra-high performance liquid chromatography–mass spectrometry (UHPLC–MS) showed higher conversion yields (%) for naringin and rutin esters using acyl donors with 8C and 10C. Rutin decanoate had higher partition coefficients (0.95), and naringin octanoate and naringin decanoate showed greater inhibitory effects on XO (IC(50) of 110.35 and 117.51 μM, respectively). Kinetic analysis showed significant differences (p < .05) between the flavonoids before and after acylation regarding K(m) values, whereas the values for V(max) were the same, implying the competitive nature of XO inhibition. |
format | Online Article Text |
id | pubmed-6445226 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-64452262019-04-09 Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically de Araújo, Maria Elisa Melo Branco Franco, Yollanda Edwirges Moreira Alberto, Thiago Grando Messias, Marcia Cristina Fernandes Leme, Camila Wielewski Sawaya, Alexandra Christine Helena Frankland Carvalho, Patricia de Oliveira J Enzyme Inhib Med Chem Research Paper Studies have reported that flavonoids inhibit xanthine oxidase (XO) activity; however, poor solubility and stability in lipophilic media limit their bioavailability and applications. This study evaluated the kinetic parameters of XO inhibition and partition coefficients of flavonoid esters biosynthesised from hesperidin, naringin, and rutin via enzymatic acylation with hexanoic, octanoic, decanoic, lauric, and oleic acids catalysed by Candida antarctica lipase B (CALB). Quantitative determination by ultra-high performance liquid chromatography–mass spectrometry (UHPLC–MS) showed higher conversion yields (%) for naringin and rutin esters using acyl donors with 8C and 10C. Rutin decanoate had higher partition coefficients (0.95), and naringin octanoate and naringin decanoate showed greater inhibitory effects on XO (IC(50) of 110.35 and 117.51 μM, respectively). Kinetic analysis showed significant differences (p < .05) between the flavonoids before and after acylation regarding K(m) values, whereas the values for V(max) were the same, implying the competitive nature of XO inhibition. Taylor & Francis 2017-07-18 /pmc/articles/PMC6445226/ /pubmed/28718686 http://dx.doi.org/10.1080/14756366.2017.1347165 Text en © 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. 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 work is properly cited. |
spellingShingle | Research Paper de Araújo, Maria Elisa Melo Branco Franco, Yollanda Edwirges Moreira Alberto, Thiago Grando Messias, Marcia Cristina Fernandes Leme, Camila Wielewski Sawaya, Alexandra Christine Helena Frankland Carvalho, Patricia de Oliveira Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title | Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title_full | Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title_fullStr | Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title_full_unstemmed | Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title_short | Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
title_sort | kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6445226/ https://www.ncbi.nlm.nih.gov/pubmed/28718686 http://dx.doi.org/10.1080/14756366.2017.1347165 |
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