Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology
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-m...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | zho |
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The editorial department of Science and Technology of Food Industry
2023-09-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2023030066 |
| _version_ | 1797690061456670720 |
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| author | Lixia ZAN Weiwei WANG Wenyi ZHANG Xinsheng LI Xiaohua CHEN Fei YAN Jing FU |
| author_facet | Lixia ZAN Weiwei WANG Wenyi ZHANG Xinsheng LI Xiaohua CHEN Fei YAN Jing FU |
| author_sort | Lixia ZAN |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-12T01:54:07Z |
| format | Article |
| id | doaj.art-5058efa6a7ff41628cc8fcb51d11a110 |
| institution | Directory Open Access Journal |
| issn | 1002-0306 |
| language | zho |
| last_indexed | 2024-03-12T01:54:07Z |
| publishDate | 2023-09-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
| record_format | Article |
| series | Shipin gongye ke-ji |
| spelling | doaj.art-5058efa6a7ff41628cc8fcb51d11a1102023-09-08T06:41:53ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062023-09-01441830030610.13386/j.issn1002-0306.20230300662023030066-18Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking TechnologyLixia ZAN0Weiwei WANG1Wenyi ZHANG2Xinsheng LI3Xiaohua CHEN4Fei YAN5Jing FU6Shaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaShaanxi University of Technology, Hanzhong 723001, ChinaObjective: 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.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2023030066ultrafiltration affinityliquid chromatography-mass spectrometrymolecular dockingtea leavesα-glucosidase inhibitory peptide |
| spellingShingle | Lixia ZAN Weiwei WANG Wenyi ZHANG Xinsheng LI Xiaohua CHEN Fei YAN Jing FU Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology Shipin gongye ke-ji ultrafiltration affinity liquid chromatography-mass spectrometry molecular docking tea leaves α-glucosidase inhibitory peptide |
| title | Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology |
| title_full | Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology |
| title_fullStr | Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology |
| title_full_unstemmed | Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology |
| title_short | Screening of α-Glucosidase Inhibitory Peptides from Tea Leaves using Ultrafiltration Affinity Combined with Liquid Chromatography-Mass Spectrometry and Molecular Docking Technology |
| title_sort | screening of α glucosidase inhibitory peptides from tea leaves using ultrafiltration affinity combined with liquid chromatography mass spectrometry and molecular docking technology |
| topic | ultrafiltration affinity liquid chromatography-mass spectrometry molecular docking tea leaves α-glucosidase inhibitory peptide |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2023030066 |
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