The hydrolysis of mussel (Mytilus edulis) protein in the presence of six different proteases was investigated. The results showed that Alcalase 2.4 L catalyzed the hydrolysis most efficiently among the tested proteases. In addition, the highest protein recovery was achieved in the case of Alcalase hydrolysate which possesses the strongest angiotensin‐i‐converting enzyme (ACE) inhibitory activity. Moreover, response surface methodology (RSM) was applied to optimize the hydrolysis conditions. The optimum values for enzyme/substrate ratio (E/S), pH and temperature were found to be 1.64%, 9.12 and 57C, respectively. Under the optimal condition, the mussel protein hydrolysate (MPHs) was prepared by Alcalase. Furthermore, the distribution of the relative molecular weight was examined by HPLC and the result showed that the oligomeric peptides peptides with molecular weight below 1,000 Da account for 78.4% of MPHs. It has been demonstrated that MPHs could serve as a source of peptides with ACE inhibitory activity and the short peptides below 1,000 Da might mainly attribute the activity to it.
PRACTICAL APPLICATION
As an important protein resource, mussel is known as nutritional food. Because of their enlarging scale and outdated process technology, the mussel has a low commercial value and the waste of mussel protein is rather serious. The expanded development of functional activity from mussel protein is very limited for lack of desirable modification process. To extend the potential health effects of mussel protein, it needs to be investigated systematically. There is only one study on the development of mussel protein as functional food. In that work, mussel protein was modified by fermentation and the resulting fermented sauces was found to possess strong angiotensin‐i‐converting enzyme (ACE) inhibitory activity, suggesting that mussel proteins may possess amino acid sequence with ACE inhibitory activity. In the present study, the mussel protein was modified by hydrolysis with various enzymes and the effect of hydrolysis condition by Alcalase on ACE inhibitory activity was extensively studied. The enzymatic hydrolysis was proven to be an efficient way to modify mussel protein. The hydrolysates obtained under the optimal hydrolysis condition showed strong ACE inhibitory activity. It is expected that the mussel protein hydrolysates with strong ACE inhibitory activity could be used as new additives in a wide range of functional foods to enhance their therapeutic properties, for instance, anti‐hypertension.