Abstract
Food protein and peptides are generally considered a source of dietary antioxidants. The antioxidant activity and peptide profiles of four extensive hydrolysates of milk protein concentrate (MPC) were examined using the two-step enzymatic method. The hydrolysis combinations were Alcalase-Flavourzyme (AE), Alcalase-ProteAXH (AH), Alcalase-Protamex (AX) and Alcalase-Protease A 2SD (AD). The results showed that highest degree of hydrolysis corresponded to the AE sample (20.41%). High-efficiency gel-filtration chromatography results indicated that the relative proportions of extensive hydrolysates with molecular weights < 3 kDa were 99.89%, 99.57%, 99.93%, and 99.89% for AX, AE, AD and AH, respectively. The hydrolysates of the MPC exhibited increased radical-scavenging capacity, as evidenced through an analysis with 1,1-diphenyl-2-pycryl-hydrazyl (DPPH), 2,2-azinobis (3-ethylbenzothiazo-line-6-sulfonic acid) diammonium salt (ABTS), reducing power and hydroxyl-radical scavenging activity testing. The main bioactive peptides were identified through EASY-nLC-orbitrap MS/MS and bioinformatics. The study may provide useful information regarding the antioxidant properties of extensive hydrolysates of MPC.
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