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Natural deep eutectic ready to use extract of astilbin: Super high in vitro bioaccessibility, α-amylase and α-glucosidase enzyme inhibition kinetics.
Xia, Hongjuan; Lv, Chenghao; Lu, Yuting; Zeng, Chaoxi; Qin, Si; Shi, Meng.
Afiliação
  • Xia H; Lab of Food Function and Nutrigenomics, College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China.
  • Lv C; College of Biological Science and Technology, Hunan Agricultural University, Changsha 410128, China.
  • Lu Y; Lab of Food Function and Nutrigenomics, College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China.
  • Zeng C; Lab of Food Function and Nutrigenomics, College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China.
  • Qin S; Lab of Food Function and Nutrigenomics, College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China. Electronic address: qinsiman@hunau.edu.cn.
  • Shi M; Lab of Food Function and Nutrigenomics, College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China. Electronic address: shimeng@hunau.edu.cn.
Food Res Int ; 173(Pt 2): 113368, 2023 11.
Article em En | MEDLINE | ID: mdl-37803707
ABSTRACT
Astilbin, a natural flavonoid, possesses multiple functionalities, while the poor bioavailability seriously restricts its application in functional food and medicine. Therefore, in this study, a natural deep eutectic solvent (NaDES) with choline chloride lactic acid (CHCL-LAC) is selected to deliver astilbin by evaluating the bioaccessibility and antioxidant capacity during in vitro gastrointestinal digestion, and the inhibitory effect with underlying mechanism of astilbin-CHCL-LAC against α-amylase/α-glucosidase were investigated. The CHCL-LAC showed significant high astilbin bioaccessibility (84.1% bioaccessible) and DPPH and ORAC antioxidant capacity with 75.7% and 57.7% respectively after 3 h in vitro digestion, which may be attributed by hydrogen bond based supramolecule formed between astilbin and CHCL-LAC. Moreover, significant inhibitions of astilbin-CHCL-LAC on α-amylase (IC50 of 0.67 g/L) and α-glucosidase (IC50 of 0.64 g/L) were observed in mixed competitive and non-competitive manners. The dominant binding force between enzymes and astilbin were the hydrogen and hydrophobic interaction. This is the first time that the underlying mechanisms for astilbin delivered by NaDESs were revealed, suggesting that CHCL-LAC-based NaDESs are promising ready-to-use vehicles of natural inhibitors for carbohydrate-hydrolyzing enzymes.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Alfa-Glucosidases / Antioxidantes Idioma: En Revista: Food Res Int Ano de publicação: 2023 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Alfa-Glucosidases / Antioxidantes Idioma: En Revista: Food Res Int Ano de publicação: 2023 Tipo de documento: Article País de afiliação: China