Antioxidant properties of porcine liver proteins hydrolyzed using Monascus purpureus

Abstract

In this study, the antioxidant activities of porcine liver proteins, hydrolyzed using Alcalase^®, papain, pepsin, or a microbial suspension of Monascus purpureus (APLH, PaPLH, PePLH, and MPLH, respectively), were investigated. The results indicated that the yield and degree of hydrolysis (DH) of hydrolysates increased with hydrolysis time. The highest yield and peptide content were obtained from APLH, whereas the DH of PaPLH was higher than that of the others. MPLH exhibited the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and reducing power, whereas APLH and PaPLH exhibited the higher ferrous ion-chelating ability than that of the MPLH. The molecular weights of all the hydrolysates were <10 kDa. The PaPLH exhibited the highest contents of total amino acids and hydrophobic amino acids. Fifteen antioxidant fractions obtained from MPLH contained one or more of the following amino acids in their sequences: Tyr, Trp, Ala, Pro, Met, Lys, Asp, Cys, Val, Leu, and His.

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