The porcine cruor represents a co-product from slaughterhouses. It mainly contains hemoglobin which is rich in bioactive peptides obtained by hydrolysis by porcine pepsin. The aim of this study is to valorize this new source rich of bioactive peptides to be used as feed additives. An in silico study on the potential of porcine cruor to contain bioactive peptides was studied by comparing it with peptides derived from bovine hemoglobin. The blast results showed a high similarity between porcine cruor hydrolysate peptides and bovine hemoglobin hydrolysates for both α and β chains with identities of 87% and 83% respectively. Cleavage sites of porcine cruor were also predicted using Peptide Cutter software and compared with bovine hemoglobin. Results reveal the preservation of most of peptides of porcine cruor hydrolysates comparing to bovine hemoglobin hydrolysates. The presence of bioactive peptides was then determined by mass spectrometry analysis. Results showed the presence of 37 bioactive peptides defined by their sequences found in previous study with mainly antibacterial and opioid peptides. The antibacterial activity was then verified by in vitro analysis against 4 bacterial strains. Results showed interesting MIC values comparing with tested synthetic peptides (4.53 µM for M.luteus and L.innocua, 35.94 µM for E.coli and 312 µM for S.newport). The antioxidant activity was also verified by studying DPPH•+ trapping and results showed an antiradical activity for porcine cruor hydrolysate greater than neokyotorphin which was previously validated as a natural preservative to substitute synthetic additives against food alteration (14% and 10% respectively). These similarities of porcine cruor hydrolysate in peptic profiles as well as biological activities make it a new interesting source of bioactive peptides.

Pseudomonas strains isolated from oil contaminated soils were screened for biosurfactant production. Three out of eleven Pseudomonas isolates were selected for their high emulsifying activity (E24 value on n-hexadecane * 78%). These isolates (E39, E311 and E313) were identified as members of the P. putida group using phenotypical methods and a molecular approach. To identify the chemical nature of produced biosurfactants, thin layer chromatography and MALDI-ToF mass spectrometry analysis were carried out and revealed lipopeptides belonging to the syringafactin family. The activity of the produced biosurfactants was stable over a pH range of 6-12, at high salinity (10%) and after heating at 80°C. Tests in contaminated sand micro-bioreactors showed that the three strains were able to degrade diesel. These results suggest the potential of these syringafactin producing strains for application in hydrocarbon bioremediation.

The hydrolysates of animal proteins from Agri-Resources have been the subject of numerous studies for their potential which makes it possible to produce molecules with high added value thanks to their richness in bioactive peptides obtained after enzymatic hydrolysis. The poultry cruor represents an important co-product from slaughterhouses. The aim of this study is to characterize this new source of peptides to be valorized as feed additives. In this work, the conditions of peptides production were fist studied, and revealed that hydrolysis and discoloration are both optimal at pH 3, and that the optimal initial substrate concentration is at 9% (w/v). The potential of poultry cruor to contain bioactive peptides was then studied in silico by comparing poultry with bovine hemoglobin derived peptides using bioinformatic tools. The blast results showed the presence of high similarities between poultry hemoglobin and bovine hemoglobin sequences with identities of 71.13% and 64.34% for α and β chains respectively. The prediction of cleavage sites of poultry hemoglobin was also carried out using peptidecutter software and compared to bovine hemoglobin peptides. The results the presence of similar peptides of poultry cruor hydrolysates comparing to bovine hemoglobin hydrolysates with generation of many new peptides. Mass spectrometry analysis was carried out to determine of bioactive peptides in poultry cruor hydrolysate based on those defined in previous studies. Results revealed the presence of 28 bioactive peptides with mainly opioid and antibacterial peptides. The antibacterial activity was then inspected in vitro against 6 different strains. Results revealed bacterial growth inhibition with interesting MIC values (10 mg/mL against M.luteus E.coli and S.aureus,1.25 mg/mL against K.rhizophilia and 20 mg/mL against S.entirica and L.innocua). The antioxidant activity was also evaluated using different tests. The β-carotene bleaching inhibition activity revealed a RAA of 79.23 ± 1.4%. The DPPH•+ trapping assay an antiradical activity of poultry cruor hydrolysate of 829.35 ± 21.12 µmol/mL and 708.85 ± 0.66 µmol/mL at 40 mg/mL and 20 mg/mL of hydrolysate respectively which is greater than BHT at 0.1 mg/mL and neokyotorphin. The ABTS radical scavenging method revealed inhibition percentages are higher than 90% for hydrolysate concentration above 10 mg/mL which are higher than those obtained with BHT at 0.5 mg/mL. and Finally, the Total antioxidant capacity (TAC) assay showed that the studied hydrolysate have a TAC comprised between that of BHT at 0.3 mg/mL and 0.1 mg/mL. Consequently, these important biological activities found in poultry cruor hydrolysate make it a new interesting alternative natural additive in food industry.