Pea protein-quercetin glycoside complexes: Interaction, foaming and emulsifying properties

Interactions of proteins and phenolics: A case for pulse proteins and onion flavonoids

“…Zhang, Wang, et al, 2022). As indicated in Roos and Subramanian theory (Ross & Subramanian, 1981), pea protein-quercetin/quercetin derivatives interaction was mainly driven by spontaneous hydrogen bonding and Van der Waals forces (ΔH˂0, ΔS˂0, and ΔG˂0) (Fu et al, 2023;X. Zhang, Wang, et al, 2022).…”

“…The maximum wavelength of soy, pea, lentil, or black bean protein (λ max ) was shifted to a lower wavelength (a blue shift) due to the proteinquercetin/onion skin extract interaction since tryptophan in the protein shifted to a hydrophobic environment. Further, a reduction in the intensity of intrinsic fluorescence of pulse proteins was reported with the increase in quercetin or onion skin extract concentration (Fu et al, 2023;Günal-Köroğlu, Yılmaz, et al, 2022;L. Han, Lu, et al, 2021;Parolia et al, 2022;X.…”

“…The development of a non-fluorescent and ground-state stable compound between the fluorophore and the quencher initiates static quenching (L. Han, Lu, et al, 2021;Liao et al, 2022). It has been emphasized that quercetin has a higher binding affinity to pulse proteins than curcumin/ resveratrol (X. , quercitrin/rutin (Fu et al, 2023), and rutin/ellagic acid (Parolia et al, 2022). Possibly, the presence of glycoside and the absence of C-3 active hydroxyl groups increased the steric hindrance of flavonoids (quercitrin and rutin) (Fu et al, 2023;Parolia et al, 2022).…”

“…It has been emphasized that quercetin has a higher binding affinity to pulse proteins than curcumin/ resveratrol (X. , quercitrin/rutin (Fu et al, 2023), and rutin/ellagic acid (Parolia et al, 2022). Possibly, the presence of glycoside and the absence of C-3 active hydroxyl groups increased the steric hindrance of flavonoids (quercitrin and rutin) (Fu et al, 2023;Parolia et al, 2022). Moreover, more hydroxyl groups in the phenolic compound and a catechol moiety of the B ring of quercetin had greater binding to the lysine side chains in proteins (Parolia et al, 2022).…”

“…This paper specifically focuses on the studies dealing with the interaction of pulse proteins with quercetin. The effects of pulse protein-quercetin or onion skin extract complexes in different matrices (emulsions and aqueous solution) as a result of incubation under certain conditions have been investigated (Chen et al, 2018;Fu et al, 2023;L. Han, Lu, et al, 2021;Liao et al, 2022;Lin et al, 2023;Parolia et al, 2022;X.…”