Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping
文献类型： 外文期刊
作者： Zhang, Jianan 1 ; Liu, Yang 3 ; Jiang, Liwen 3 ; Zhao, Tiantian 4 ; Su, Guowan 1 ; Zhao, Mouming 1 ;
作者机构： 1.South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Peoples R China
2.Guangdong Food Green Proc & Nutr Regulat Technol R, Guangzhou 510650, Peoples R China
3.Hunan Agr Univ, Coll Food Sci & Technol, Changsha 410125, Peoples R China
4.Guangdong Acad Agr Sci, Guangdong Key Lab Agr Prod Proc, Minist Agr & Rural Affairs, Sericulture & Agrifood Res Inst,Key Lab Funct Food, Guangzhou 510610, Peoples R China
关键词： elastin peptides; 2D LC-MS; peptide fingerprinting; enzymatic cleavage patterns; elastase inhibitory activity
期刊名称：MOLECULES （ 影响因子：4.6； 五年影响因子：4.9 ）
ISSN：
年卷期： 2023 年 28 卷 22 期
页码：
收录情况： SCI
摘要： To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate's bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase (R) 2.4L's preference for these residues. The analysis not only confirms the peptides' dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin.
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