Enzymatic Production of Novel European Eel Proteins Hydrolysates: Biological Activities, Techno-Functional Properties and Maltodextrin-Hydrolysates Efficient Electrosprayability

European eel proteins hydrolysates (EPHs) were produced from A. anguilla muscle protein and protein isolate using Purafect (R), goby crude proteases and B. invictae proteases. EPHs had high protein contents and displayed diverse molecular mass distributions. Muscle protein hydrolysates (MPHs) and protein isolate hydrolysates (PIHs) obtained both by Purafect (R) had the highest antibacterial activity. PIHs obtained by B. invictae proteases had the highest emulsifying stability. MPHs and PIHs obtained by goby proteases and PIHs obtained by B. invictae proteases had higher chelating effects. MPHs obtained by B. invictae proteases and PIHs obtained by Purafect (R) had the highest ability to prevent bleaching of beta-carotene at 4 mg/ml (96.68% and 93.66% respectively). The maltodextrin-muscle protein hydrolysates dispersions were totally stable by the creaming index and the zeta potential values (-36.73 and -42.53 mV) compared to the maltodextrin-protein isolate hydrolysates dispersions and had the best electrosprayability approving the best ability to form microcapsules.

Automated summary

European eel proteins hydrolysates were produced using different proteases, showing that hydrolysates obtained by Purafect (R) had highest antibacterial activity, while those obtained by B. invictae proteases exhibited superior emulsifying stability.