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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Bibliographic Details
Published in:Journal of Enzyme Inhibition and Medicinal Chemistry
Main Authors: 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
Format: Text
Language:English
Published: Taylor & Francis 2017
Subjects:
Research Paper
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6445226/
http://www.ncbi.nlm.nih.gov/pubmed/28718686
https://doi.org/10.1080/14756366.2017.1347165
Description
Summary: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.

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