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Inhibitory effects of phenolic compounds from blueberry leaf on α-amylase and α-glucosidase: kinetics, mode of action, and molecular interactions

文献类型： 外文期刊

作者： Wu, Han 1 ; Liu, Xiaoli 1 ; Xie, Shudong 1 ; Zhou, Jianzhong 1 ; Corradini, Maria G. 3 ; Pan, Yue 1 ; Cui, Xiaozhen 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Agroprod Proc, 50 Zhongling St, Nanjing 210014, Jiangsu, Peoples R China

2.Minist Agr & Rural Affairs, Key Lab Cold Chain Logist Technol Agroprod, Nanjing, Peoples R China

3.China Canada Smart Proc Res Ctr Enhencing Food Int, Nanjing, Peoples R China

4.Univ Guelph, Dept Food Sci, Guelph, ON, Canada

关键词： blueberry leaf; digestive enzymes; kinetics; inhibition mechanism; multispectral technique

期刊名称：JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE （ 影响因子：3.5； 五年影响因子：4.2 ）

ISSN： 0022-5142

年卷期： 2025 年 105 卷 8 期

页码：

收录情况： SCI

摘要： Background: The interactions between blueberry leaf polyphenols (BLPs) and digestive enzymes were analyzed using multiple techniques to gain insights into their inhibitory effects on enzyme kinetics and modes of action. Results: 3-O-Caffeoylquinic acid (3-CQA) was the most abundant compound identified. Quercetin (QR) exhibited the strongest inhibitory activity against alpha-amylase (alpha-AMY) and alpha-glucosidase (alpha-GLU). The BLP extracts acted as typical mixed-type inhibitors for both digestive enzymes, showing stronger inhibition of alpha-GLU (IC50 = 7.36 +/- 0.03 mu g mL(-1)) than alpha-AMY (IC50 = 12.52 +/- 0.65 mu g mL(-1)). Stern-Volmer plots showed static quenching of enzyme fluorescence intensity. The quenching and binding constants of alpha-GLU were higher than those of alpha-AMY, showing greater affinity of the former for BLP. The conformational changes of 3-CQA and QR in the BLP were studied at the molecular level. The stability of the complexes formed followed this order: alpha-GLU-3-CQA > alpha-AMY-QR > alpha-GLU-QR > alpha-AMY-3-CQA. This trend supported the observation that QR had a greater impact on alpha-AMY conformation, whereas 3-CQA more effectively altered alpha-GLU. Conclusion: These findings elucidated the inhibitory mechanisms of BLP on glucose-regulating enzymes, providing novel insights relevant for the treatment of diabetes. (c) 2025 Society of Chemical Industry.

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