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Authors

CHEN Bing-bing, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
YANG Yi, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
LI Jia-yi, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
JIN Chang-yan, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
CHENG Bin-pei, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
DENG Yong-qi, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
LIN Bi-min, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China
LIANG Dong, State Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources,Guangxi Normal University, Guilin, Guangxi 541004 , China
TANG De-jian, Key Laboratory of Se-enrichedProducts Development and Quality Control, Ministry of Agriculture and Rural Affairs/National-LocalJoint Engineering Laboratory of Se-enriched Food Development, Ankang, Shaanxi 725000 , China ;Ankang R&D Center for Se-enriched Products, Ankang, Shaanxi 725000 , China
MENG Li, Key Laboratory of Se-enrichedProducts Development and Quality Control, Ministry of Agriculture and Rural Affairs/National-LocalJoint Engineering Laboratory of Se-enriched Food Development, Ankang, Shaanxi 725000 , China ;Ankang R&D Center for Se-enriched Products, Ankang, Shaanxi 725000 , China
MIAO Jian-yin, College of Food Science South China Agricultural University, Guangzhou, Guangdong 510642 ,China

Abstract

Objective: To develop selenium-enriched (Se-enriched) Moringa oleifera seed protein resources. Methods: Using Se-enriched Moringa oleifera seed protein powder as raw material, the enzymatic hydrolysis conditions of Se-enriched Moringa oleifera seed protein antihypertensive peptides from Se-enriched Moringa oleifera seed protein were obtained by single factor and response surface optimization, and the ACE inhibitory activity, Se content and stability of the optimal enzymatic hydrolysate were analyzed. Results: The optimal enzymatic hydrolysis conditions of Se-enriched Moringa oleifera were as follows: enzymatic hydrolysis time 3 h, temperature 34 ℃, pH 8, concentration of substrate 7%, enzyme to substrate ratio 0.3%. Under these conditions, the semi-inhibitory concentration of ACE of the peptides was 1.956 mg/mL. The Se content of the antihypertensive peptide was 1.394 mg/kg, which was 1.1 times that of the raw protein. Moreover, the antihypertensive peptides (5 mg/mL) had good thermal stability and acid-base stability, and could still maintain good ACE inhibitory activity after digestion by gastrointestinal enzyme system in vitro. Conclusion: The Se-enriched Moringa oleifera seed protein antihypertensive peptides obtained by response surface optimization showed strong ACE inhibitory activity and good stability.

Publication Date

10-16-2022

First Page

213

Last Page

221

DOI

10.13652/j.spjx.1003.5788.2022.90140

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