Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct
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-pe...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2022-11-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453022001069 |
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| author | Qiang Wu Changqing Zhong Guirong Zeng Xu Zhang Liping Xiang Chang Wan Yougui Yu |
| author_facet | Qiang Wu Changqing Zhong Guirong Zeng Xu Zhang Liping Xiang Chang Wan Yougui Yu |
| author_sort | Qiang Wu |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-891d15de262f482f8f3e257a688f54d8 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2022-11-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-891d15de262f482f8f3e257a688f54d82025-02-03T06:56:02ZengTsinghua University PressFood Science and Human Wellness2213-45302022-11-0111616411649Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproductQiang Wu0Changqing Zhong1Guirong Zeng2Xu Zhang3Liping Xiang4Chang Wan5Yougui Yu6College of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, ChinaDepartment of Cardiovascular Medicine, Hunan Provincial People's Hospital, Changsha 410005, China; Corresponding authors.Hunan Experimental Animal Center, Hunan Drug Safety Evaluation and Research Center, Liuyang 410331, ChinaCollege of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, ChinaCollege of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, ChinaCollege of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, ChinaCollege of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, China; Corresponding authors.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.http://www.sciencedirect.com/science/article/pii/S2213453022001069BaijiuDistilled spent grainACE inhibitory peptideInhibition mechanism |
| spellingShingle | Qiang Wu Changqing Zhong Guirong Zeng Xu Zhang Liping Xiang Chang Wan Yougui Yu Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct Food Science and Human Wellness Baijiu Distilled spent grain ACE inhibitory peptide Inhibition mechanism |
| title | Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct |
| title_full | Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct |
| title_fullStr | Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct |
| title_full_unstemmed | Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct |
| title_short | Identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct |
| title_sort | identification and characterization of a novel tetrapeptide from enzymatic hydrolysates of baijiu byproduct |
| topic | Baijiu Distilled spent grain ACE inhibitory peptide Inhibition mechanism |
| url | http://www.sciencedirect.com/science/article/pii/S2213453022001069 |
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