1. Inhibitory Effect of Antidesma bunius Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
- Author
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Thavaree Thilavech, Charoonsri Choosak, Sathaporn Ngamukote, Kittana Mäkynen, Marisa Marnpae, Winai Dahlan, Sirichai Adisakwattana, Netima Chamnansilpa, and Pattamaporn Aksornchu
- Subjects
0301 basic medicine ,Antioxidant ,antioxidant ,Physiology ,DPPH ,medicine.medical_treatment ,Clinical Biochemistry ,Trolox equivalent antioxidant capacity ,Biochemistry ,protein glycation ,Sucrase ,03 medical and health sciences ,chemistry.chemical_compound ,Glycation ,medicine ,Food science ,Molecular Biology ,Antidesma bunius ,030109 nutrition & dietetics ,biology ,Chemistry ,lcsh:RM1-950 ,food and beverages ,Cell Biology ,biology.organism_classification ,anthocyanins ,α-amylase ,030104 developmental biology ,lcsh:Therapeutics. Pharmacology ,α-glucosidase ,Maltase ,Ellagic acid - Abstract
Antidesma bunius (L.) spreng (Mamao) is widely distributed in Northeastern Thailand. Antidesma bunius has been reported to contain anthocyanins, which possess antioxidant and antihypertensive actions. However, the antidiabetic and antiglycation activity of Antidesma bunius fruit extract has not yet been reported. In this study, we investigated the inhibitory activity of anthocyanin-enriched fraction of Antidesma bunius fruit extract (ABE) against pancreatic &alpha, amylase, intestinal &alpha, glucosidase (maltase and sucrase), protein glycation, as well as antioxidant activity. A liquid chromatography-tandem mass spectrometry (LC-MS/MS) chromatogram revealed that ABE contained phytochemical compounds such as cyanidin-3-glucoside, delphinidin-3-glucoside, ellagic acid, and myricetin-3-galactoside. ABE inhibited intestinal maltase and sucrase activity with the IC50 values of 0.76 ±, 0.02 mg/mL and 1.33 ±, 0.03 mg/mL, respectively. Furthermore, ABE (0.25 mg/mL) reduced the formation of fluorescent AGEs and the level of N&epsilon, carboxymethyllysine (N&epsilon, CML) in fructose and glucose-induced protein glycation during four weeks of incubation. During the glycation process, the protein carbonyl and &beta, amyloid cross structure were decreased by ABE (0.25 mg/mL). In addition, ABE exhibited antioxidant activity through DPPH radical scavenging activity and Trolox equivalent antioxidant capacity (TEAC) with the IC50 values 15.84 ±, 0.06 µ, g/mL and 166.1 ±, 2.40 µ, g/mL, respectively. Meanwhile, ferric reducing antioxidant power (FRAP) showed an EC50 value of 182.22 ±, 0.64 µ, g/mL. The findings suggest that ABE may be a promising agent for inhibiting carbohydrate digestive enzyme activity, reducing monosaccharide-induced protein glycation, and antioxidant activity.
- Published
- 2021