Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism
The purpose of this study was to prepare a novel Angiotensin-I-Converting Enzyme(ACE) inhibitory peptide by hydrolyzing sheep casein with protease and analyze its molecular inhibitory mechanism, so as to provide technical support for the development of functional sheep milk polypeptide dairy product...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | zho |
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The editorial department of Science and Technology of Food Industry
2022-01-01
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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.issn1002-0306.2021040014 |
| _version_ | 1828134553750863872 |
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| author | Haixia TANG Shuangshuang WANG Guo HAO Yuxun SONG Lei ZHANG Wupeng GE |
| author_facet | Haixia TANG Shuangshuang WANG Guo HAO Yuxun SONG Lei ZHANG Wupeng GE |
| author_sort | Haixia TANG |
| collection | DOAJ |
| description | The purpose of this study was to prepare a novel Angiotensin-I-Converting Enzyme(ACE) inhibitory peptide by hydrolyzing sheep casein with protease and analyze its molecular inhibitory mechanism, so as to provide technical support for the development of functional sheep milk polypeptide dairy products. In this experiment, sheep casein was used as raw material, with hydrolysis degree, ACE inhibition rate and molecular weight distribution as indexes, the most suitable protease was selected from four proteases, and the components with less than <3 kDa was identified by LTQ Orbitrap Velos mass spectrometer. the potential ACE inhibitory peptides were selected for artificial synthesis and it half inhibitory concentration (IC50) was measured. The inhibition kinetics of enzyme was determined by Linewaver-Burk mapping, and the inhibition mechanism of peptide segment was further explained by molecular docking. The results showed that alkaline protease was the best hydrolytic protease. A new ACE inhibitory peptide KYIPIQY was screened from κ -casein and its IC50 was 5.73 μmol/L. Linewaver-Burk diagram showed that the peptide showed a mixed inhibition mode on ACE. Molecular docking showed that KYIPIQY can form hydrogen bonds with S1 and S2 active pockets of ACE, and closely combine with hydrophobic force. KYIPIQY can distort the Zn2+ tetrahedron of ACE, and inhibit the deactivation of ACE catalytic activity, thus exerting high-efficiency ACE inhibitory activity. |
| first_indexed | 2024-04-11T17:37:16Z |
| format | Article |
| id | doaj.art-f36f156d287143c48fef87ada7287e62 |
| institution | Directory Open Access Journal |
| issn | 1002-0306 |
| language | zho |
| last_indexed | 2024-04-11T17:37:16Z |
| publishDate | 2022-01-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
| record_format | Article |
| series | Shipin gongye ke-ji |
| spelling | doaj.art-f36f156d287143c48fef87ada7287e622022-12-22T04:11:35ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062022-01-0143111011810.13386/j.issn1002-0306.20210400142021040014-1Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding MechanismHaixia TANG0Shuangshuang WANG1Guo HAO2Yuxun SONG3Lei ZHANG4Wupeng GE5College of Food Science and Engineering, Northwest A & F University, Yangling 712100, ChinaCollege of Food Science and Engineering, Northwest A & F University, Yangling 712100, ChinaShaanxi Goat Milk Product Quality Supervision and Inspection Center, Fuping 711700, ChinaCollege of Animal Science and Technology, Northwest A & F University, Yangling 712100, ChinaCollege of Animal Science and Technology, Northwest A & F University, Yangling 712100, ChinaCollege of Food Science and Engineering, Northwest A & F University, Yangling 712100, ChinaThe purpose of this study was to prepare a novel Angiotensin-I-Converting Enzyme(ACE) inhibitory peptide by hydrolyzing sheep casein with protease and analyze its molecular inhibitory mechanism, so as to provide technical support for the development of functional sheep milk polypeptide dairy products. In this experiment, sheep casein was used as raw material, with hydrolysis degree, ACE inhibition rate and molecular weight distribution as indexes, the most suitable protease was selected from four proteases, and the components with less than <3 kDa was identified by LTQ Orbitrap Velos mass spectrometer. the potential ACE inhibitory peptides were selected for artificial synthesis and it half inhibitory concentration (IC50) was measured. The inhibition kinetics of enzyme was determined by Linewaver-Burk mapping, and the inhibition mechanism of peptide segment was further explained by molecular docking. The results showed that alkaline protease was the best hydrolytic protease. A new ACE inhibitory peptide KYIPIQY was screened from κ -casein and its IC50 was 5.73 μmol/L. Linewaver-Burk diagram showed that the peptide showed a mixed inhibition mode on ACE. Molecular docking showed that KYIPIQY can form hydrogen bonds with S1 and S2 active pockets of ACE, and closely combine with hydrophobic force. KYIPIQY can distort the Zn2+ tetrahedron of ACE, and inhibit the deactivation of ACE catalytic activity, thus exerting high-efficiency ACE inhibitory activity.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021040014sheep milkcaseinace inhibitory peptideinhibitory kineticsmolecular docking |
| spellingShingle | Haixia TANG Shuangshuang WANG Guo HAO Yuxun SONG Lei ZHANG Wupeng GE Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism Shipin gongye ke-ji sheep milk casein ace inhibitory peptide inhibitory kinetics molecular docking |
| title | Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism |
| title_full | Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism |
| title_fullStr | Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism |
| title_full_unstemmed | Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism |
| title_short | Identification of a Novel ACE-inhibitory Peptide from Sheep Casein and Evaluation of the Molecular Binding Mechanism |
| title_sort | identification of a novel ace inhibitory peptide from sheep casein and evaluation of the molecular binding mechanism |
| topic | sheep milk casein ace inhibitory peptide inhibitory kinetics molecular docking |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021040014 |
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