Inhibition of beta-carotene-15,15 ‘-dioxygenase activity by dietary flavonoids
Sommaire de l'article
Beta-Carotene-15, 15'-dioxygenase is an enzyme responsible for providing vertebrates with vitamin A by catalyzing oxidative cleavage of beta-carotene at its central double bond to two molecules of retinal in intestinal cells. However, little data have been reported regarding regulation of the enzyme activity.
We have evaluated the effects of antioxidants and dietary flavonoids on the beta-carotene dioxygenase activity in vitro using a pig intestinal homogenate as the enzyme source. 2,6-Di-tert-butyl-4-methylphenol (BHT), a synthetic antioxidant, strongly inhibited the activity at the level of 10(-6) M (a mixed-type inhibition), whereas butylated hydroxyanisole nor-dihydroguaiaretic acid, n-propyl gallate, and curcumin were moderately inhibitory.
Flavonoids such as luteolin, quercetin, rhamnetin, and phloretin remarkably inhibited the dioxygenase activity noncompetitively whereas flavanones, isoflavones, catechins, and anthocyanidins were less inhibitory. The structure-activity relationship indicated that catechol structure of ring B and a planar flavone structure were essential for inhibition. The enzyme inhibition was also indicated in the cultured Caco-2 cells by the significantly reduced conversion of beta-carotene to retinol when incubated with BHT and rhamnetin at 2 mu M and 5 mu M, respectively.
The results suggest that some dietary antioxidants derived from food sources modulate conversion of beta-carotene to vitamin A in intestinal cells.