The aim of this study was to investigate the phenolic profiles, antioxidant activities and α-glycosidase inhibitory activities of three different phenolic fractions from water caltrop (Trapa quadrispinosa Roxb.) husk and to further explore the predominant compounds and their mechanisms on α-glycosidase inhibition by virtual screening and molecular dynamics. A total of 29 substances were identified and quantified in this study. Tannins were the main constituents of water caltrop husk extract. All of the free phenolic (FP), esterified phenolic (EP) and insoluble-bound phenolic (BP) fractions exhibited good antioxidant activities, and the BP had the highest radical scavenging ability with IC50 values of 0.82 ± 0.12 μg/mL (ABTS) and 1.15 ± 0.02 μg/mL (DPPH), respectively (p < 0.05). However, compared with the EP and BP, the FP showed the strongest inhibition towards the α-glycosidase and the IC50 value of FP was 1.43 ± 0.12 μg/mL. The 1,2,6-trigalloylglucose and α-glycosidase complex had better root mean square deviations (RMSD) stability via molecular dynamics simulation study. Results obtained from this study may provide a good potential natural resource for the improvement of oxidative stress injury and blood glucose control in diabetes mellitus, which could expand the use of water caltrop husk and improve its economic value.

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Prinsepia utilis Royle (P. utilis) is commonly used as a food ingredient and herbal medicine according to folk records, yet little research has been done on the seed shell, a processing waste. The aim of this study was to investigate the distribution of polyphenolic components and the tyrosinase activation activity of different extracts from the seed shell by UHPLC-ESI-HRMS/MS, in vitro tyrosinase activity assay, molecular docking and molecular dynamics. A total of 16 phytochemicals were identified, of which (+)-catechin and (−)-epicatechin were the major polyphenolic compounds. Both the esterified and insoluble bound polyphenols exhibited tyrosinase activation activity, and the esterified polyphenols showed better tyrosinase activation activity. (+)-Catechin and (−)-epicatechin might be the main activators of tyrosinase, both of which may act as substrate to affect tyrosinase activity. By molecular docking and molecular dynamics simulation studies, (+)-catechin and (−)-epicatechin can be efficiently and stably bound to the tyrosinase active site through hydrogen bonds, van der Waals forces and π-bonds. The results of this study may not only provide a scientific basis for exploring P. utilis seed shell as a potential activator of tyrosinase, but also contribute to the high value utilization of P. utilis processing by-products.