ACE inhibitory and antioxidant activities of red scorpionfish (Scorpaena notata) protein hydrolysates

Abstract

Fish protein hydrolysates with different degrees of hydrolysis were prepared from muscle and heads of red scorpionfish (Scorpaena notata) by treatment with different proteases (Flavourzyme, Trypsin from bovine pancreas and crude enzyme preparations from the intestines of red scorpionfish and from the fungus Penicillium digitatum). The antioxidant and the antihypertensive activities of the hydrolysates were tested. The antioxidant power was evaluated through DPPH free radical scavenging activity, reducing power and metal chelating activity. All hydrolysates showed different degrees of hydrolysis and varying degrees of antioxidant activity. The hydrolysates obtained by treatment with crude enzyme preparations exhibited the highest antioxidant activity. Further, red scorpionfish head protein hydrolysates obtained with fungal protease and with fish crude protease were found to strongly inhibit the angiotensin-I converting enzyme (IC 50 of 0.489 and 0.901 mg/ml, respectively). These results suggested that hydrolysates of red scorpionfish obtained by treatment with crude enzyme preparations would be a beneficial ingredient for functional food or pharmaceuticals against hypertension.

Optimal Production of Protein Hydrolysates from Monkfish By-Products: Chemical Features and Associated Biological Activities

“…The values of in vitro antioxidants of monkfish hydrolysates were less active and valuable than compared with the data of the hydrolysates from herring, hoki, and trout [ 38 , 39 , 40 ], but showed similar values of DPPH (around 50%) than those recently reported for the head of L. vomerinus [ 23 ]. The present bioactivities are also in line with the results reported in FPH generated from discarded fish and turbot by-products [ 14 , 41 , 42 , 43 ]. Identical findings of DPPH inhibition percentage were defined for collagen derivatives obtained from the enzyme digestion of fin and skin of salmon [ 44 , 45 ].…”

Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Razor Clam Sinonovacula constricta

“…On the other hand, using this enzyme may also cause degradation of active peptides into shorter inactive peptides or amino acids. Similar inefficiency of using flavourzyme in the production of ACE-inhibitory peptides was reported for red scorpion fish proteins [ 34 ].…”

Development of bioprocesses for the integral valorisation of fish discards

“…Altough we consider that AO activities were generally low when they are compared with synthetic and natural antioxidants [49][50][51][52] and other bioactive peptides produced from marine waste effluents and fish by-products [6,15,16,[53][54][55][56], our levels are in the same order of magnitude than those found by FPHs from whole BW obtained using Alcalase [57] and from head RS hydrolysed with Trypsin and Flavourzyme [58].…”