Investigation of the interaction for three Citrus flavonoids and α-amylase by surface plasmon resonance. (July 2017)

• Record Type: Journal Article
• Authors: Liu, Xia; Luo, Fang; Li, Pao; She, Yin; Gao, Wanru
• Is Part Of: Food research international. Volume 97(2017)
• Page Start: 1
• Page End: 6
• Publication Date: 2017-07
• Subjects: Naringin (PubChem CID: 442428) -- Neohesperidin (PubChem CID: 442439) -- Hesperidin (PubChem CID: 10621) -- Acarbose (PubChem CID: 122172882) -- Atrazine (PubChem CID: 2256); Citrus flavonoids -- α-Amylase -- Interaction -- Surface plasmon resonance biosensor -- DPPH; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2017.03.023
• Languages: English
• ISSNs: 0963-9969

Abstract

Abstract: Flavonoids, a class of natural drugs with broad biological activity, exhibit inhibitory effect on α-amylase. Citrus peel is a good source of flavonoids. The real-time interactions between three Citrus flavonoids (naringin, neohesperidin, hesperidin) and α-amylase were investigated by surface plasmon resonance biosensor, and were compared with the α-amylase inhibitors, acarbose. These results showed the binding affinities of naringin, neohesperidin and hesperidin with α-amylase reach the highest at pH 6 with KD values of 2.27 ± 0.18 mM, 3.09 ± 0.20 mM and 3.51 ± 0.09 mM, and can be reinforced with 0.2 M NaCl and 0.1 M CaCl2, respectively. The results of 1, 1-diphenyl-2-picryl hydrazyl radical assay indicate that the antioxidant activities of naringin, neohesperidin and hesperidin are significantly inhibited by interacting with α-amylase, and the inhibition percentage are 47.61 ± 0.034%, 22.81 ± 0.037% and 21.01 ± 0.051%, respectively. Additionally, it is found that both the number and the position of hydroxyl group play an important role in the interaction of three Citrus flavonoids and α-amylase. These results provide useful information for rapid screening inhibitors of α-amylase from plant-based food. Graphical abstract: Highlights: The real-time interactions of hesperidin, neohesperidin, naringin with α-amylase were investigated using SPR biosensor. Affinities of three flavonoids to α-amylase are the highest at pH 6, can be reinforced with 0.2 M NaCl or 0.1 M CaCl2 . Binding of three flavonoids to α-amylase induced the decrease of their antioxidant activities. Binding of three flavonoids to α-amylase depends strongly on both the number and position of hydroxyl group.