食品科学 ›› 2026, Vol. 47 ›› Issue (19): 75-84.doi: 10.7506/spkx1002-6630-20260318-134

• 基础研究 • 上一篇    

聚酯型儿茶素A的制备及其对糖脂代谢相关酶的抑制作用

刘佳,赵欣蕊,付静,杨晨曦   

  1. (1.陕西理工大学生物科学与工程学院,陕西 汉中 723000;2.陕西省资源生物重点实验室,陕西 汉中 723000;3.陕西理工大学 秦巴生物资源与生态环境省部共建国家重点实验室(培育),陕西 汉中 723000)
  • 发布日期:2026-10-22
  • 基金资助:
    陕西省重点研发计划项目(2024QY2-GJHX-18)

Preparation of Theasinensin A and Its Inhibitory Effects on Enzymes Associated with Glucose and Lipid Metabolism

LIU Jia, ZHAO Xinrui, FU Jing, YANG Chenxi   

  1. (1. College of Biological Science and Engineering, Shaanxi University of Technology, Hanzhong 723000, China; 2. Shaanxi Province Key Laboratory of Bio-resources, Hanzhong 723000, China; 3. Qinba State Key Laboratory of Biological Resources and Ecological Environment (Incubation), Shaanxi University of Technology, Hanzhong 723000, China)
  • Published:2026-10-22

摘要: 针对聚酯型儿茶素A(theasinensin A,TSA)在茶叶中提取困难的问题,本研究利用丰水梨多酚氧化酶(polyphenol oxidase,PPO)低温催化表没食子儿茶素没食子酸酯(epigallocatechin gallate,EGCG)氧化生成TSA,再经动态轴向压缩色谱分离纯化获得高纯度TSA单体,并系统评价其对糖脂代谢相关酶的抑制作用及体外模拟消化特性。结果表明,本研究制得的TSA纯度最高,为98.92%,分子质量为914 Da,分子式为C44H34O22;核磁共振(nuclear magnetic resonance,NMR)氢谱、碳谱及二维谱分析进一步确证了TSA的对称二聚体结构。TSA对α-淀粉酶的半数抑制浓度(half-maximal inhibitory concentration,IC50)为(0.34±0.01)mg/mL,最高抑制率达(86.45±0.78)%,显著优于EGCG和阿卡波糖(P<0.05),对α-葡萄糖苷酶的抑制率在测试浓度范围内均低于50%(IC50>100 μg/mL);对脂肪酶和胆固醇酯酶的IC50分别为(29.96±2.28)mg/mL和(32.77±2.54)mg/mL,最高抑制率分别达(73.79±1.74)%和(81.00±2.17)%,显著优于EGCG和奥利司他(P<0.05)。体外模拟消化结果表明,TSA对α-淀粉酶和脂肪酶的抑制活性呈现口腔和胃消化阶段较高、小肠消化阶段显著降低的阶段依赖性规律,与TSA二聚体结构赋予的较高消化稳定性有关。本研究可为TSA的绿色高效提取及其功能产品开发提供理论依据。

关键词: 聚酯型儿茶素A;低温酶法合成;动态轴向压缩色谱;糖脂代谢酶;抑制作用;体外模拟消化

Abstract: To overcome the difficulty of isolating theasinensin A (TSA) from tea, polyphenol oxidase (PPO) extracted from Fengshui pears was employed to catalyze the low-temperature oxidative conversion of epigallocatechin gallate (EGCG) into TSA. High-purity TSA was subsequently obtained by dynamic axial compression chromatography. Its inhibitory effects on enzymes involved in carbohydrate and lipid metabolism, as well as its behavior during in vitro simulated digestion, were systematically evaluated. The results showed that the purity of the prepared TSA was as high as 98.92%. TSA had a molecular mass of 914 Da and a molecular formula of C44H34O22. One-dimensional proton nuclear magnetic resonance spectroscopy (1H NMR) and carbon-13 nuclear magnetic resonance spectroscopy ( 13C NMR), together with two-dimensional NMR analysis, confirmed its symmetric dimeric structure. The half-maximal inhibitory concentration (IC50) of TSA against α-amylase was (0.34 ± 0.01) mg/mL, and its maximum inhibitory rate reached (86.45 ± 0.78)%, which was significantly higher than those of EGCG and acarbose (P < 0.05). The inhibitory rate of TSA against α-glucosidase remained below 50% throughout the tested concentration range, with an IC50 value greater than 100 μg/mL. The IC50 values of TSA against lipase and cholesterol esterase were (29.96 ± 2.28) and (32.77 ± 2.54) mg/mL, with maximum inhibitory rates of (73.79 ± 1.74)% and (81.00 ± 2.17)%, respectively. These inhibitory effects were significantly stronger than those of EGCG and orlistat (P < 0.05). In vitro simulated digestion showed that the inhibitory activities of TSA against α-amylase and lipase varied with digestion stages, remaining relatively high during the oral and gastric phases but decreasing significantly during the intestinal phase. This pattern may be attributed to the relatively high digestive stability conferred by the dimeric structure of TSA. These findings provide a theoretical basis for the green and efficient preparation of TSA and its potential application in the development of functional food products.

Key words: theasinensin A; low-temperature enzymatic synthesis; dynamic axial compression chromatography; glucose and lipid metabolic enzymes; inhibitory effect; in vitro simulated digestion

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