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Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

文献类型： 外文期刊

作者： Chen, Yu 1 ; Zhang, Yu 2 ; Qi, Qianhui 2 ; Liang, Feng 2 ; Wang, Nan 6 ; Chen, Qihe 7 ; Li, Xue 2 ; Sun, Suling 2 ; Wang, Xinquan 2 ; Bai, Kaiwen 8 ; Wang, Wei 2 ; Jiao, Yingchun 1 ;

作者机构： 1.Qinghai Univ, Coll Agr & Anim Husb, Xining, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Agr Safety & Nutr, Hangzhou, Peoples R China

3.Minist Agr & Rural Affairs China, Key Lab Agr Prod Informat Traceabil, Hangzhou, Peoples R China

4.Zhejiang Prov Key Lab Food Safety, Hangzhou, Peoples R China

5.Bohai Univ, Coll Food Sci & Engn, Jinzhou, Peoples R China

6.Zhejiang Shuren Univ, Hangzhou, Peoples R China

7.Zhejiang Univ, Sch Biol Syst Engn & Food Sci, Hangzhou, Peoples R China

8.Zhejiang Univ Sci & Technol, Sch Biol & Chem Engn, Hangzhou, Peoples R China

关键词： mulberry leaf protein; hydrolysate; angiotensin-I converting enzyme (ACE); inhibitory peptides; molecular docking

期刊名称：FRONTIERS IN NUTRITION （ 影响因子：5.0； 五年影响因子：5.7 ）

ISSN： 2296-861X

年卷期： 2023 年 9 卷

页码：

收录情况： SCI

摘要： Angiotensin-I converting enzyme (ACE) inhibitory peptides drew wide attention in the food industry because of their natural reliability, non-toxicity, and safety. However, the characteristics of ACE inhibitory peptides obtained from protein hydrolysate of mulberry leaf prepared by Flavourzyme were still unclear. Based on the single-factor test, the Plackett-Burman test and response surface test were used to determine the key factors affecting the ACE inhibition rate in mulberry leaf protein hydrolysate and the optimum conditions of enzymatic hydrolysis. The results showed that the optimum technical parameters were as follows: the ratio of material to liquid is 1: 25 (w / v, g/mL), the Flavourzyme to substrate ratio was 3,000 U/g, the temperature of enzymatic hydrolysis was 50 degrees C, pH was 6.3, and the time of enzymatic hydrolysis was 2.9 h. The ACE inhibitory peptides in the mulberry leaf protein hydrolysates were purified by ultrafiltration and gel filtration, aiming to obtain the highest active component. The 12 peptide sequences were identified by reverse liquid chromatography-mass spectrometry, and then, they were docked to the crystal structure of human angiotensin-I converting enzyme (1O8A), and the interaction mechanisms of 12 peptide sequences and 1O8A were analyzed. The docking results showed that among the 12 peptide sequences, ERFNVE (792.37 Da), TELVLK (351.72 Da), MELVLK (366.72 Da), and FDDKLD (376.67 Da), all had the lowest docking energy, and inhibition constant. The chemosynthetic ERFNVE (IC50: 2.65 mg/mL), TELVLK (IC50: 0.98 mg/mL), MELVLK (IC50:1.90 mg/mL) and FDDKLD (IC50:0.70 mg/mL) demonstrated high ACE-inhibitory activity with competitive inhibition mode. These results indicated that the ACE-inhibiting peptides from mulberry leaf protein hydrolyzed (FHMP) had the potential activities to inhibit ACE and could be used as functional food or drugs to inhibit ACE. This work provides positive support for mining the biological activity of mulberry leaves in the treatment of hypertension.

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