Preparation, purification, and identification of novel antioxidant peptides derived from Gracilariopsis lemaneiformis protein hydrolysates.

ABSTRACT: Gracilariopsis lemaneiformis (G. lemaneiformis) protein was hydrolyzed with alkaline protease to obtain antioxidant peptides. The enzymatic hydrolysis conditions were optimized through single-factor and orthogonal experiments. The results showed that the optimal process parameters were using 2% of alkaline protease, and substrate concentration of 1 g/100 mL and hydrolyzed 2 h at pH 8.0. Gel filtration chromatography and RP-HPLC were adopted for isolating and purifying the antioxidant peptides from the G. lemaneiformis protein hydrolysate (GLPH). Three novel antioxidant peptides were identified as LSPGEL (614.68 Da), VYFDR (698.76 Da), and PGPTY (533.57 Da) by nano-HPLC-MS/MS. The results of ABTS free radical scavenging rate demonstrated PGPTY exhibited the best antioxi

SUBMITTER: Hu X 

PROVIDER: S-EPMC9355161 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature