Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro

<i>Antidesma bunius</i> (L.) spreng (Mamao) is widely distributed in Northeastern Thailand. <i>Antidesma bunius</i> has been reported to contain anthocyanins, which possess antioxidant and antihypertensive actions. However, the antidiabetic and antiglycation activity of <i...

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Main Authors: Pattamaporn Aksornchu, Netima Chamnansilpa, Sirichai Adisakwattana, Thavaree Thilavech, Charoonsri Choosak, Marisa Marnpae, Kittana Mäkynen, Winai Dahlan, Sathaporn Ngamukote
Format: Article
Language:English
Published: MDPI AG 2020-12-01
Series:Antioxidants
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Online Access:https://www.mdpi.com/2076-3921/10/1/32
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author Pattamaporn Aksornchu
Netima Chamnansilpa
Sirichai Adisakwattana
Thavaree Thilavech
Charoonsri Choosak
Marisa Marnpae
Kittana Mäkynen
Winai Dahlan
Sathaporn Ngamukote
author_facet Pattamaporn Aksornchu
Netima Chamnansilpa
Sirichai Adisakwattana
Thavaree Thilavech
Charoonsri Choosak
Marisa Marnpae
Kittana Mäkynen
Winai Dahlan
Sathaporn Ngamukote
author_sort Pattamaporn Aksornchu
collection DOAJ
description <i>Antidesma bunius</i> (L.) spreng (Mamao) is widely distributed in Northeastern Thailand. <i>Antidesma bunius</i> has been reported to contain anthocyanins, which possess antioxidant and antihypertensive actions. However, the antidiabetic and antiglycation activity of <i>Antidesma bunius</i> fruit extract has not yet been reported. In this study, we investigated the inhibitory activity of anthocyanin-enriched fraction of <i>Antidesma bunius</i> fruit extract (ABE) against pancreatic α-amylase, intestinal α-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 IC<sub>50</sub> 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<sup>ε</sup>-carboxymethyllysine (N<sup>ε</sup>-CML) in fructose and glucose-induced protein glycation during four weeks of incubation. During the glycation process, the protein carbonyl and β-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 IC<sub>50</sub> values 15.84 ± 0.06 µg/mL and 166.1 ± 2.40 µg/mL, respectively. Meanwhile, ferric reducing antioxidant power (FRAP) showed an EC<sub>50</sub> value of 182.22 ± 0.64 µg/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.
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spelling doaj.art-b9b773d57631481da76054534cee28742023-11-21T03:07:43ZengMDPI AGAntioxidants2076-39212020-12-011013210.3390/antiox10010032Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In VitroPattamaporn Aksornchu0Netima Chamnansilpa1Sirichai Adisakwattana2Thavaree Thilavech3Charoonsri Choosak4Marisa Marnpae5Kittana Mäkynen6Winai Dahlan7Sathaporn Ngamukote8Phytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandDepartment of Food Chemistry, Faculty of Pharmacy, Mahidol University, Bangkok 10400, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, ThailandThe Halal Science Center, Chulalongkorn University, Bangkok 10330, ThailandPhytochemical and Functional Food Research Unit for Clinical Nutrition, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand<i>Antidesma bunius</i> (L.) spreng (Mamao) is widely distributed in Northeastern Thailand. <i>Antidesma bunius</i> has been reported to contain anthocyanins, which possess antioxidant and antihypertensive actions. However, the antidiabetic and antiglycation activity of <i>Antidesma bunius</i> fruit extract has not yet been reported. In this study, we investigated the inhibitory activity of anthocyanin-enriched fraction of <i>Antidesma bunius</i> fruit extract (ABE) against pancreatic α-amylase, intestinal α-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 IC<sub>50</sub> 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<sup>ε</sup>-carboxymethyllysine (N<sup>ε</sup>-CML) in fructose and glucose-induced protein glycation during four weeks of incubation. During the glycation process, the protein carbonyl and β-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 IC<sub>50</sub> values 15.84 ± 0.06 µg/mL and 166.1 ± 2.40 µg/mL, respectively. Meanwhile, ferric reducing antioxidant power (FRAP) showed an EC<sub>50</sub> value of 182.22 ± 0.64 µg/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.https://www.mdpi.com/2076-3921/10/1/32α-amylaseα-glucosidase<i>Antidesma bunius</i>protein glycationanthocyaninsantioxidant
spellingShingle Pattamaporn Aksornchu
Netima Chamnansilpa
Sirichai Adisakwattana
Thavaree Thilavech
Charoonsri Choosak
Marisa Marnpae
Kittana Mäkynen
Winai Dahlan
Sathaporn Ngamukote
Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
Antioxidants
α-amylase
α-glucosidase
<i>Antidesma bunius</i>
protein glycation
anthocyanins
antioxidant
title Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
title_full Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
title_fullStr Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
title_full_unstemmed Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
title_short Inhibitory Effect of <i>Antidesma bunius</i> Fruit Extract on Carbohydrate Digestive Enzymes Activity and Protein Glycation In Vitro
title_sort inhibitory effect of i antidesma bunius i fruit extract on carbohydrate digestive enzymes activity and protein glycation in vitro
topic α-amylase
α-glucosidase
<i>Antidesma bunius</i>
protein glycation
anthocyanins
antioxidant
url https://www.mdpi.com/2076-3921/10/1/32
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