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中国精品科技期刊2020
昝丽霞,王威威,张文夷,等. 超滤亲和结合液相色谱-质谱联用和分子对接技术筛选茶叶中α-葡萄糖苷酶抑制肽[J]. 食品工业科技,2023,44(18):300−306. doi: 10.13386/j.issn1002-0306.2023030066.
引用本文: 昝丽霞,王威威,张文夷,等. 超滤亲和结合液相色谱-质谱联用和分子对接技术筛选茶叶中α-葡萄糖苷酶抑制肽[J]. 食品工业科技,2023,44(18):300−306. doi: 10.13386/j.issn1002-0306.2023030066.
ZAN Lixia, WANG Weiwei, ZHANG Wenyi, et al. Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology[J]. Science and Technology of Food Industry, 2023, 44(18): 300−306. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023030066.
Citation: ZAN Lixia, WANG Weiwei, ZHANG Wenyi, et al. Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology[J]. Science and Technology of Food Industry, 2023, 44(18): 300−306. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023030066.

超滤亲和结合液相色谱-质谱联用和分子对接技术筛选茶叶中α-葡萄糖苷酶抑制肽

Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology

  • 摘要: 目的:筛选茶叶中具有抑制α-葡萄糖苷酶活性的肽段。方法:采用响应面法优化茶叶酶解产物制备工艺,超滤亲和法分离与α-葡萄糖苷酶结合的茶多肽,液相色谱-质谱联用对分离肽段进行序列测定,生物信息学方法进行虚拟筛选。结果:茶叶酶解产物最佳制备工艺为碱性蛋白酶酶解温度50 ℃,酶解时间3 h,液料比10:1 (mL/g),对α-葡萄糖苷酶抑制率为57.29%,从中鉴定出624条肽段,筛选出一条四肽LIGF具有α-葡萄糖苷酶抑制活性,在 5 mg/mL的浓度下对α-葡萄糖苷酶的最大抑制率为88.13%,IC50值为1.22 mg/mL。分子对接显示,LIGF与α-葡萄糖苷酶能形成5个氢键,结合能为−3.51 kJ,具有高的亲和力、稳定性以及与α-葡萄糖苷酶结合的能力。结论:LIGF具有成为II型糖尿病治疗药物的潜在价值。

     

    Abstract: Objective: To screen for tea peptides with inhibitory activity against α-glucosidase. Methods: The response surface method was used to optimize the preparation process of tea peptides. Affinity ultrafiltration was used to isolate tea peptides that bind with α-glucosidase, and liquid chromatography-mass spectrometry was used to determine the sequence of the isolated peptides. Virtual screening was performed using bioinformatics methods. Results: The optimal preparation process of tea leaf enzymatic hydrolysis products was alkaline protease hydrolysis temperature of 50 ℃, enzymatic hydrolysis time of 3 h, and a liquid-to-solid ratio of 10:1 (mL/g). The α-glucosidase inhibitory rate was 57.29%. From this, 624 peptide segments were identified, and LIGF was selected for its α-glucosidase inhibitory activity. At a concentration of 5 mg/mL, LIGF exhibited a maximum inhibition rate of 88.13% against α-glucosidase and an IC50 value of 1.22 mg/mL. Molecular docking showed that LIGF could form 5 hydrogen bonds with α-glucosidase, and the binding energy was −3.51 kJ, indicating a high affinity, stability and ability to bind to α-glucosidase. Conclusion: LIGF had potential value as a therapeutic drug for type II diabetes.

     

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