Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-47484
Food Chem February 15, 2020; 306 125581.

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.

Zhang Y , He S , Bonneil É , Simpson BK .


Abstract
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.

PubMed ID: 31606636
Article link: Food Chem