Chemical and biological characterization of spirulina protein hydrolysates: Focus on ACE and DPP-IV activities modulation

被引:42
作者
Aiello, Gilda [1 ]
Li, Yuchen [1 ]
Boschin, Giovanna [1 ]
Bollati, Carlotta [1 ]
Arnoldi, Anna [1 ]
Lammi, Carmen [1 ]
机构
[1] Univ Milan, Dept Pharmaceut Sci, Via Mangiagalli 25, I-20133 Milan, Italy
关键词
ACE; Caco-2; cells; DPP-IV; Bioactive peptides; Peptidomic; Spirulina protein; DIPEPTIDYL-PEPTIDASE IV; INHIBITORY PEPTIDES; ENZYMATIC-HYDROLYSIS; BIOACTIVE PEPTIDES; CONVERTING-ENZYME; LUPIN; PHYCOCYANIN; EXTRACTION; MICROALGAE; DIGEST;
D O I
10.1016/j.jff.2019.103592
中图分类号
TS2 [食品工业];
学科分类号
100403 [营养与食品卫生学];
摘要
Microalgae are considered a viable source of protein and among them spirulina (Arthrospira platensis) stands out for its exceptionally high protein content and its potential nutraceutical properties. In the present work, peptic (SP) and tryptic (ST) protein hydrolysates were produced using pepsin and trypsin, respectively. The kinetics of peptides release from the protein were investigated and the hydrolysates composition was assessed by HPLC-ESI-MS/MS, identifying 55 and 76 species-specific peptides in the SP and ST hydrolysates, respectively. The bioactivity was investigated by performing in vitro experiments and cellular assays in Caco-2 cells. SP and ST inhibited in vitro the activity of peptidyl-peptidase IV (DPP-IV) with IC50 of 3.4 and 0.1 mg/mL, respectively, and of angiotensin converting enzyme (ACE) with IC50 of 3.0 and 0.28 mg/mL. Both activities were confirmed in Caco-2 cells, although their further metabolic degradation reduced their potencies.
引用
收藏
页数:8
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