Composition and biological activities of slaughterhouse blood from red deer, sheep, pig and cattle.

BACKGROUND: Animal blood is a large-volume by-product of the meat industry. Besides blood meal fertiliser, blood is marketed for human consumption as a supplement. Minimal comparative work on slaughterhouse animal blood fractions has been carried out. In this study, slaughterhouse deer, sheep, pig and cattle blood parameters were compared. Some blood constituents were determined. Fractionated blood was assessed for antioxidant activity (2,2-diphenyl-1-picrylhydrazyl radical scavenging, oxygen radical scavenging capacity and ferric reducing antioxidant power). Angiotensin converting enzyme (ACE) inhibitory activity and antimicrobial activity were also assessed. RESULTS: Serum iron ranged from 35.3 ± 0.6 µmol L(-1) in cattle to 16.3 ± 3.1 µmol L(-1) in deer. Cattle had the highest total plasma proteins (81.7 ± 1.5 g L(-1)). While the plasma fractions contained considerable antioxidant activity, the red blood cell fractions of all four animal species contained higher antioxidant activity (P < 0.05). Negligible levels of ACE inhibitory activity were found for all animal blood fractions. Antimicrobial activity was detected towards Escherichia coli, Staphylococcus aureus and Pseudomonas aeruginosa with sheep white blood cells from which a crude neutrophil extract was obtained which demonstrated concentration-dependent inhibitory effects on the growth rates of these bacterial strains. CONCLUSION: Fractionated animal blood obtained from local slaughterhouses contains native proteins that possess antioxidant activity and antimicrobial activity.

Generation of bioactive peptide hydrolysates from cattle plasma using plant and fungal proteases.

Four protease preparations from plant and fungal sources (papain, bromelain, FP400 and FPII) were used to hydrolyse plasma which was separated from slaughterhouse cattle blood. The o-phthaldialdehyde assay was used to follow the release of TCA-soluble peptides over a 24h period. Hydrolysis profiles were displayed using SDS-PAGE. The in vitro antioxidant and antimicrobial activities of the hydrolysates were determined. The results showed that hydrolysates of cattle plasma generated with fungal protease FPII had higher antioxidant activities. Overall than hydrolysates generated with papain, bromelain and FP400. None of the hydrolysates demonstrated antimicrobial activity. The FPII peptide hydrolysate was fractionated using gel permeation chromatography, OFFGEL isoelectric focusing and RP-HPLC. The RP-HPLC fraction with highest antioxidant activity contained 15 novel peptide sequences. The use of protease FPII to hydrolyse cattle plasma resulted in a hydrolysate with high antioxidant properties and unique peptide sequences.

Production of bioactive peptide hydrolysates from deer, sheep, pig and cattle red blood cell fractions using plant and fungal protease preparations.

Protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) sources were used to hydrolyze the red blood cell fractions (RBCFs) separated from deer, sheep, pig, and cattle abattoir-sourced blood. After 1, 2, 4 and 24h of hydrolysis, the antioxidant and antibacterial activities of the peptide hydrolysates obtained were investigated. The increase in trichloroacetic acid-soluble peptides over the hydrolysis period was examined using the o-phthaldialdehyde (OPA) assay and the hydrolysis profiles were illustrated using SDS-PAGE. Papain generated RBCF hydrolysates exhibited higher ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) compared to those generated with bromelain, FP400 and FPII. At certain concentrations, 24h hydrolysates of RBCF using FP400 and FPII were able to inhibit the growth of Escherichia coli, Staphylococcus aureus and Pseudomonas aeruginosa. The results indicated that the use of proteases from plant or fungal sources can produce animal blood hydrolysates with antioxidant and antimicrobial activities.

Production of bioactive peptide hydrolysates from deer, sheep and pig plasma using plant and fungal protease preparations.

Plasma separated from deer, sheep and pig blood, obtained from abattoirs, was hydrolysed using protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) sources. Antioxidant and antimicrobial activities of the peptide hydrolysates obtained after 1, 2, 4 and 24h of hydrolysis, were investigated. The release of trichloroacetic acid-soluble peptides over the hydrolysis period was monitored using the o-phthaldialdehyde (OPA) assay, while the hydrolysis profiles were visualised using SDS-PAGE. The major plasma proteins in the animal plasmas were identified using MALDI-TOF-TOF MS. Hydrolysates of plasma generated with fungal proteases exhibited higher DPPH radical-scavenging, oxygen radical-scavenging capacity (ORAC) and ferric reducing antioxidant power (FRAP) than those generated with plant proteases for all three animal plasmas. No antimicrobial activity was detected in the hydrolysates. The results indicated that proteolytic hydrolysis of animal blood plasmas, using fungal protease preparations in particular, produces hydrolysates with high antioxidant properties.