Antioxidant activity of hydrolysates derived from porcine plasma

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Abstract

BACKGROUND: In China alone, more than 400 million pigs are slaughtered each year to provide meat. Porcine blood is rich in proteins but is usually discarded, which can cause environmental contamination. Recovering porcine blood and converting it to high-value products is therefore economically and environmentally desirable. However, very little information on antioxidant peptides from porcine blood by-products is currently available. In this study the antioxidant properties of porcine plasma hydrolysates PPE and PPA prepared with pepsin and papain respectively were investigated.

RESULTS: Both PPE and PPA showed excellent antioxidant activity in a linoleic acid system (AL) compared with α-tocopherol (VE) at the same concentration (P < 0.01). Their activities were respectively 3.33 and 1.83 times stronger than that of VE at a concentration of 10 µg mL−1 and 5.4 and 5.6 times stronger at 100 µg mL−1. The 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical-scavenging activity (DRSA) reached 48.4 and 43.1% for PPE and PPA respectively at 500 µg mL−1. The ferrous ion-chelating power (FICP) of PPE at 100 µg mL−1 was about 1.5 times stronger than that of 10 µmol L−1 ethylene diamine tetraacetic acid (EDTA) in a 50 µmol L−1 Fe2+ system, whereas the FICP of PPA at 100 µg mL−1 was 61% that of 10 µmol L−1 EDTA. Furthermore, PPE was separated on Resource 15RPC and Superdex peptide 10/300GL columns, and the antioxidant activity of the peptides and its relationship to their polarity and molecular weight (MW) were analysed. The hydrolysate was divided into four groups (R1–R4) with hydrophobicities ranging from weak to strong by Resource 15RPC, while it was divided into three groups (S1, MW 7–12 kDa; S2, MW 3–7 kDa; S3, MW 1–3 kDa) by Superdex peptide 10/300GL.

CONCLUSION: The results showed that AL was significantly and positively correlated with the relative amounts of R1, S2 and S3 and that DRSA was dependent on R3 and S1. The fractions of PPE were not responsible for FICP. Copyright © 2009 Society of Chemical Industry

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