In this study, sheep plasma was submitted to Alcalase-hydrolysis and peptides with better antioxidant properties measured through both the ferric-reducing antioxidant power (FRAP) and the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging ability assays were isolated and identified. After hydrolysate ultrafiltration and semi-preparative reverse-phase high-performance liquid chromatography, nine fractions (F1–F9) were obtained, with the two first (F1 and F2) showing the greatest antioxidant potential. These two fractions were further separated by the AKTA purifier system to generate four (F1-1–F1-4) and five (F2-1–F2-5) fractions, respectively, with two of them (F1-2 and F2-1) exhibiting appreciable FRAP activity and DPPH radical scavenging ability. Using liquid chromatography-tandem mass spectrometry, three antioxidant peptides were identified. From their amino acid sequences (QTALVELLK, SLHTLFGDELCK, and MPCTEDYLSLILNR), which include amino acids that have been previously reported as key contributors to the peptide antioxidant properties, it can be maintained that they come mainly from serum albumin. These results suggested that the sheep plasma protein can be considered as a good source of antioxidant peptides and bring forth new possibilities for the utilization of animal blood by-products.
Porcine blood plasma is a rich source of proteins with high nutritional and functional properties, which can be used as a food ingredient. The plasma is usually processed into powders in applications. In the present study, the effects of drying methods and ash contents on heat-induced gelation of plasma protein powder were investigated. The drying methods had a significant impact on the gel properties of the plasma powder heat-induced gels. The hardness and elasticity of the gels by freeze-dried and spray-dried plasma powders were lower than that of the liquid plasma (p < 0.05). The microstructures of dehydrated plasma were denser and the holes were smaller. The secondary structure of the gels from the spray-dried plasma protein powders exhibited more α-helixes and less β-turns than that from the freeze-dried powder and liquid plasma. The thermostability of dehydrated plasma powder was found to have decreased compared to the liquid plasma. Compared with the gels obtained from the high ash content plasma protein powders, the gel from the 6% ash content plasma powder had the highest water-holding capacity and had the lowest hardness and elasticity. However, the secondary structure and microstructures of the heat-induced gels were not affected by the ash contents in the plasma powders. These findings show that the gel properties of plasma protein powder can be finely affected by drying methods and ash contents.
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