Novel Antioxidant Peptides from Grateloupia livida Hydrolysates: Purification and Identification.

ABSTRACT: Grateloupia livida protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates obtained by neutral protease 1 h hydrolysis displayed the highest antioxidant activity (DPPH IC₅₀ value of 3.96 mg/mL ± 0.41 mg/mL, ABTS IC₅₀ value of 0.88 ± 0.13 mg/mL and reducing power of 0.531 ± 0.012 at 8 mg/mL), and had low molecular weight distribution (almost 99% below 3 kDa). Three fractions (F1-F3) were then isolated from the hydrolysates by using semi-preparative RP-HPLC, and the fraction F3 showed the highest antioxi

SUBMITTER: Hu X 

PROVIDER: S-EPMC9141318 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature