摘要
Collagen peptides were investigated in-vitro as potential inhibitors of lipoxygenase,trypsin and monoamine oxidases(MAO),and proteins thermal denaturation.When overexpressed or dysregulated,those enzymes,and denatured proteins,mediate several inflammatory mechanisms,and also neurodegenerative diseases.Besides,they can compromise food and drugs storage.Several synthetic and plant compounds were investigated and applied as inhibitors;however,research on bioactive peptides is lagging behind,in particular if animal-derived.In this study,collagen was extracted from bovine bone by a French National Research Institute for Agriculture,Food and Environment(INRAE)patented process,and hydrolysed afterwards.Three endopeptidases were considered-bromelain,collagenase and papain-since they generate peptides that inhibit several oxidative species,which are linked to inflammation,cognitive decline,and loss of quality in several products.Two ratios enzyme/collagen(E/C),1/20 and 1/50(w/w),and two peptides sizes,≤1000 Da and≤3000,were considered.For the E/C 1/50,≤1000 Da fraction,the synergy among peptides generated by the three proteases was eval-uated.Significant biological activity emerged,which was mainly linked to the collagen protease specificity instead of peptides concentration.Lipoxygenase was inhibited by all the peptides,and those from collagenase showed the most important effect.Modulation of the trypsin activity was noticed;complete inhibition was obtained when the trypsin substrate was albumin.When that was casein,papain was the most effective protease,while bromelain and collagenase derived peptides increased the trypsin activity;this effect disappeared when peptides fractions were mixed.Only papain derived peptides were able to inhibit MAO.Outcome of this research can be considered encouraging for the investigated application.
