Dual-enzyme hydrolysis for preparation of ACE-inhibitory peptides from sesame seed protein: Optimization, separation, and identification
文献类型: 外文期刊
第一作者: Lu, Xin
作者: Lu, Xin;Sun, Qiang;Zhang, Lixia;Wang, Ruidan;Gao, Jinhong;Jia, Cong;Huang, Jinian
作者机构:
关键词: angiotensin converting enzyme inhibitors; bioactive peptides; enzymatic hydrolyzate; sesame seed protein fraction
期刊名称:JOURNAL OF FOOD BIOCHEMISTRY ( 影响因子:2.72; 五年影响因子:2.543 )
ISSN: 0145-8884
年卷期: 2021 年 45 卷 4 期
页码:
收录情况: SCI
摘要: To prepare and identify ACE-inhibitory peptides originated from sesame seed protein, peptides with strong ACE-inhibitory activities were obtained via the optimization of protease and hydrolysis conditions, and these peptides were purified and identified by membrane separation, gel filtration, and liquid chromatography-mass spectrometry. Results showed that the dual-enzyme comprised alcalase and trypsin with the enzyme activity ratio of 3:7 was suitable to produce ACE-inhibitory peptides. The highest ACE-inhibitory activity of 98.10 +/- 0.26% was obtained at the following parameters, pH 8.35, E/S ratio of 6,145 U/g, and hydrolysis time of 4.4 hr. ISGAQPSLR and VVISAPSK ranked the first and second ACE-inhibitory activity among 15 identified ACE-inhibitory peptides. Both peptides influenced ACE via binding with the S1 pocket, S2 pocket, and Zn2+ ion. ISGAQPSLR even impacted the S1 ' pocket. ISGAQPSLR and VVISAPSK acted as a competitive and noncompetitive inhibitor, respectively. ACE-inhibitory peptides derivated from sesame seed protein have potential applications in functional food. Practical applications Although sesame seed protein is proven as the precursor of ACE-inhibitory peptide, preparing ACE-inhibitory peptide from sesame seed protein is still suffering from insufficient information on hydrolysis condition and the peptide sequence. Therefore, the performance of the typical protease on preparing ACE-inhibitory peptide from sesame seed protein has been evaluated, the effect of the amino acid composition of sesame seed protein and cleavage specificity of protease on the generation of ACE-inhibitory peptide has been investigated, hydrolysis conditions have been optimized, the peptide sequence has been identified to illuminate the effect of sesame seed protein fraction on the formation of ACE-inhibitory peptide and discuss the structural characteristics. ACE-inhibitory peptides originating from sesame seed protein could apply in functional food. It is promising for dual-enzyme hydrolysis to utilize in preparation of high-value bioactive peptides.
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