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...
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ftdoajarticles:oai:doaj.org/article:6bfaba307fe74baea7f68e4664d062ac 2023-05-15T13:53:51+02:00 Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically Maria Elisa Melo Branco de Araújo Yollanda Edwirges Moreira Franco Thiago Grando Alberto Marcia Cristina Fernandes Messias Camila Wielewski Leme Alexandra Christine Helena Frankland Sawaya Patricia de Oliveira Carvalho 2017-01-01T00:00:00Z https://doi.org/10.1080/14756366.2017.1347165 https://doaj.org/article/6bfaba307fe74baea7f68e4664d062ac EN eng Taylor & Francis Group http://dx.doi.org/10.1080/14756366.2017.1347165 https://doaj.org/toc/1475-6366 https://doaj.org/toc/1475-6374 1475-6366 1475-6374 doi:10.1080/14756366.2017.1347165 https://doaj.org/article/6bfaba307fe74baea7f68e4664d062ac Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 978-985 (2017) Acylation lipase flavonoids xanthine oxidase Therapeutics. Pharmacology RM1-950 article 2017 ftdoajarticles https://doi.org/10.1080/14756366.2017.1347165 2022-12-31T01:25:13Z 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 (IC50 of 110.35 and 117.51 μM, respectively). Kinetic analysis showed significant differences (p < .05) between the flavonoids before and after acylation regarding Km values, whereas the values for Vmax were the same, implying the competitive nature of XO inhibition. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Journal of Enzyme Inhibition and Medicinal Chemistry 32 1 978 985 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
language |
English |
topic |
Acylation lipase flavonoids xanthine oxidase Therapeutics. Pharmacology RM1-950 |
spellingShingle |
Acylation lipase flavonoids xanthine oxidase Therapeutics. Pharmacology RM1-950 Maria Elisa Melo Branco de Araújo Yollanda Edwirges Moreira Franco Thiago Grando Alberto Marcia Cristina Fernandes Messias Camila Wielewski Leme Alexandra Christine Helena Frankland Sawaya Patricia de Oliveira Carvalho Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
topic_facet |
Acylation lipase flavonoids xanthine oxidase Therapeutics. Pharmacology RM1-950 |
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 (IC50 of 110.35 and 117.51 μM, respectively). Kinetic analysis showed significant differences (p < .05) between the flavonoids before and after acylation regarding Km values, whereas the values for Vmax were the same, implying the competitive nature of XO inhibition. |
format |
Article in Journal/Newspaper |
author |
Maria Elisa Melo Branco de Araújo Yollanda Edwirges Moreira Franco Thiago Grando Alberto Marcia Cristina Fernandes Messias Camila Wielewski Leme Alexandra Christine Helena Frankland Sawaya Patricia de Oliveira Carvalho |
author_facet |
Maria Elisa Melo Branco de Araújo Yollanda Edwirges Moreira Franco Thiago Grando Alberto Marcia Cristina Fernandes Messias Camila Wielewski Leme Alexandra Christine Helena Frankland Sawaya Patricia de Oliveira Carvalho |
author_sort |
Maria Elisa Melo Branco de Araújo |
title |
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_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_sort |
kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically |
publisher |
Taylor & Francis Group |
publishDate |
2017 |
url |
https://doi.org/10.1080/14756366.2017.1347165 https://doaj.org/article/6bfaba307fe74baea7f68e4664d062ac |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 978-985 (2017) |
op_relation |
http://dx.doi.org/10.1080/14756366.2017.1347165 https://doaj.org/toc/1475-6366 https://doaj.org/toc/1475-6374 1475-6366 1475-6374 doi:10.1080/14756366.2017.1347165 https://doaj.org/article/6bfaba307fe74baea7f68e4664d062ac |
op_doi |
https://doi.org/10.1080/14756366.2017.1347165 |
container_title |
Journal of Enzyme Inhibition and Medicinal Chemistry |
container_volume |
32 |
container_issue |
1 |
container_start_page |
978 |
op_container_end_page |
985 |
_version_ |
1766259305824124928 |