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In order to prepare angiotensin Ⅰ-converting enzyme (ACE) inhibitory peptides, distilled spent grains of Chinese strong-flavor Baijiu were hydrolyzed by alcalase followed by papain under optimized conditions. A superior ACE inhibitory peptide was separated and purified by ultrafiltration and high-performance liquid chromatography (HPLC), and its amino acid sequence was further identified as Gln-Gly-Val-Pro (QGVP) by electrospray mass spectrometry (ESI-MS). QGVP formed 6 hydrogen bonds with the active site of ACE, which is responsible for reducing α-helix structure content of ACE causing subsequent inactivation. Moreover, it showed no significant cytotoxicity toward human umbilical vein endothelial cells (HUVECs), and significantly induced phosphorylation of endothelial nitric oxide synthase (p-eNOS) and decreased endothelin 1 (END1) expression in angiotensin Ⅰ (Ang Ⅰ)-treated HUVECs, demonstrating the potential antihypertensive effect. The peptide QGVP hydrolyzed from distilled spent grain proteins of Chinese strong-flavor Baijiu was expected to be used as a food ingredient to prevent or co-treat hypertension with other chemical drugs.


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Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct

Show Author's information Qiang WuaChangqing Zhongb( )Guirong ZengcXu ZhangaLiping XiangaChang WanaYougui Yua( )
College of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, China
Department of Cardiovascular Medicine, Hunan Provincial People's Hospital, Changsha 410005, China
Hunan Experimental Animal Center, Hunan Drug Safety Evaluation and Research Center, Liuyang 410331, China

Peer review under responsibility of KeAi Communications Co., Ltd.

Abstract

In order to prepare angiotensin Ⅰ-converting enzyme (ACE) inhibitory peptides, distilled spent grains of Chinese strong-flavor Baijiu were hydrolyzed by alcalase followed by papain under optimized conditions. A superior ACE inhibitory peptide was separated and purified by ultrafiltration and high-performance liquid chromatography (HPLC), and its amino acid sequence was further identified as Gln-Gly-Val-Pro (QGVP) by electrospray mass spectrometry (ESI-MS). QGVP formed 6 hydrogen bonds with the active site of ACE, which is responsible for reducing α-helix structure content of ACE causing subsequent inactivation. Moreover, it showed no significant cytotoxicity toward human umbilical vein endothelial cells (HUVECs), and significantly induced phosphorylation of endothelial nitric oxide synthase (p-eNOS) and decreased endothelin 1 (END1) expression in angiotensin Ⅰ (Ang Ⅰ)-treated HUVECs, demonstrating the potential antihypertensive effect. The peptide QGVP hydrolyzed from distilled spent grain proteins of Chinese strong-flavor Baijiu was expected to be used as a food ingredient to prevent or co-treat hypertension with other chemical drugs.

Keywords: Inhibition mechanism, ACE inhibitory peptide, Baijiu, Distilled spent grain

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Publication history

Received: 29 July 2021
Revised: 05 September 2021
Accepted: 23 November 2021
Published: 18 July 2022
Issue date: November 2022

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© 2022 Beijing Academy of Food Sciences.

Acknowledgements

Acknowledgment

This study was sponsored by the Outstanding Youth Project of Hunan Education Department (19B505), Changsha City Science and Technology Plan Project (kq2004113), the 2020 Natural Science Foundation of Hunan Province of China (2020JJ8061), the 2020 Science and Technology Innovation Project of Hunan Province of China (2020SK50921) and the Undergraduate Inquiry Learning and Innovative Experimental Project of Hunan Education Department (2019[100]-1886).

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This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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