Generation of antioxidative peptides from Atlantic sea cucumber using alcalase versus trypsin: In vitro activity, de novo sequencing, and in silico docking for in vivo function prediction

被引：93

作者：

Zhang, Yi ^{[1
]}

He, Shudong ^{[2
]}

Bonneil, Eric ^{[3
]}

Simpson, Benjamin K. ^{[1
]}

机构：

[1] McGill Univ, Dept Food Sci & Agr Chem, Ste Anne De Bellevue, PQ H9X 3V9, Canada

[2] Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Anhui, Peoples R China

[3] Univ Montreal, Inst Res Immunol & Canc, Montreal, PQ, Canada

来源：

FOOD CHEMISTRY | 2020年 / 306卷

基金：

加拿大自然科学与工程研究理事会;

关键词：

Sea cucumber; Antioxidant; Alcalase; Trypsin; Peptides; Myeloperoxidase; Molecular docking; AMINO-ACID-COMPOSITION; PROXIMATE COMPOSITION; PROTEIN HYDROLYSATE; BY-PRODUCTS; MYELOPEROXIDASE; IDENTIFICATION; PURIFICATION; INHIBITION; MECHANISMS;

D O I：

10.1016/j.foodchem.2019.125581

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

A comprehensive evaluation was conducted to compare the generation of antioxidative peptides produced by alcalase versus trypsin from Atlantic sea cucumber. The in vitro antioxidative peptides were sequenced by de novo sequencing using LC-MS/MS. Key constituent antioxidative amino acids (KCAAA), i.e., Cys, His, Met, Trp and Tyr in the peptides and the molecular interactions between peptides and myeloperoxidase (MPO, a mediator and marker of in vivo oxidative stress), were analyzed by in silico methods. Alcalase-produced protein hydrolysates showed 5-35% higher in vitro antioxidant activity than the trypsin-produced ones. UPLC analysis revealed the total amino acid composition in peptide fractions < 2 kDa. Alcalase produced 35.4% of peptides with both KCAAA and potential MPO inhibitory activity, compared with only 30.3% for trypsin. A representative peptide sequence TEFHLL generated by alcalase had intense molecular interactions with MPO active site, predicting a capacity to inhibit in vivo oxidative stress.

引用

页数：10