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

ZAN Lixia; WANG Weiwei; ZHANG Wenyi; LI Xinsheng; CHEN Xiaohua; YAN Fei; FU Jing

doi:10.13386/j.issn1002-0306.2023030066

Volume 44 Issue 18

Sep. 2023

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Science and Technology of Food Industry > 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.

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

ZAN Lixia^{1, 2, 3, 4, 5, 6, ,},
WANG Weiwei¹,
ZHANG Wenyi¹,
LI Xinsheng^{1, 5, 6},
CHEN Xiaohua^{1, 5, 6},
YAN Fei^{1, 5, 6},
FU Jing^{1, 5, 6}

1.
Shaanxi University of Technology, Hanzhong 723001, China
2.
Shaanxi Province Key Laboratory of Bio-resources, Hanzhong 723001, China
3.
Qinba Mountain Area Collaborative Innovation Center of Bioresources Comprehensive Development, Hanzhong 723001, China
4.
Qinba State Key Laboratory of Biological Resources and Ecological Environment (Incubation), Hanzhong 723001, China
5.
Tea Planting and Processing Institute, Shaanxi University of Technology, Hanzhong 723001, China
6.
Shaanxi Provincial Joint Research Center for Tea Industry, Hanzhong 723001, China

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Received Date: March 05, 2023
Available Online: July 17, 2023

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Abstract

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.
- ultrafiltration affinity,
- liquid chromatography-mass spectrometry,
- molecular docking,
- tea leaves,
- α-glucosidase inhibitory peptide

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References

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

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