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. M oreover, it showed no significant cytotoxicity toward human umbilical vein endothelial cells (HUVECs), a nd significantly i nduced 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.

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

[1]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)[J].食品科学与人类健康（英文）,2022(06):1641-1649

tetrapeptide,Baijiu,alcalase,QGVP,oreover,nduced,END1

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