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1.
Food Funct ; 7(9): 3890-901, 2016 Sep 14.
Article in English | MEDLINE | ID: mdl-27526864

ABSTRACT

Fish protein hydrolysates from Mediterranean horse mackerel were produced by using a mixture of two commercial endoproteases (i.e. subtilisin and trypsin) at different levels of substrate concentration (2.5 g L(-1), 5 g L(-1), and 7.5 g L(-1) of protein), temperature (40 °C, 47.5 °C, and 55 °C) and percentage of subtilisin in the enzyme mixture (0%, 25%, 50%, 75% and 100%). A crossed mixture process model was employed to predict the degree of hydrolysis (DH) and the ACE inhibitory activity of the final hydrolysates as a function of the experimental factors. Both models were optimized for a maximum DH and ACE inhibition. A maximum DH (17.1%) was predicted at 2.54 g L(-1) of substrate concentration, 40 °C and an enzyme mixture comprising 38.3% of subtilisin and 61.7% of trypsin. Although its proteolytic activity is limited, the presence of trypsin in the enzyme mixture allowed obtaining higher degrees of hydrolysis at low temperatures, which is desirable to minimize thermal deactivation of the proteins. Similarly, a percentage of ACE inhibition above 48% was attained at 2.5 g L(-1) of protein, 40 °C and a 1 : 1 mixture of both proteases. Higher values of ACE inhibition could be attained by increasing both the temperature and the amount of trypsin in the enzyme mixture (e.g. 50% ACE inhibition at 55 °C and 81.5% of trypsin). Finally, those hydrolysates exhibiting the highest levels of ACE inhibition were subjected to simulated gastrointestinal digestion. These assays confirmed the resistance of active fractions against their degradation by digestive enzymes.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Fish Proteins/isolation & purification , Models, Biological , Protein Hydrolysates/isolation & purification , Angiotensin-Converting Enzyme Inhibitors/economics , Angiotensin-Converting Enzyme Inhibitors/metabolism , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Digestion , Fish Proteins/economics , Fish Proteins/metabolism , Fish Proteins/pharmacology , Fisheries/economics , Freeze Drying , Hot Temperature , Industrial Waste/analysis , Industrial Waste/economics , Kinetics , Mediterranean Sea , Peptidyl-Dipeptidase A/chemistry , Peptidyl-Dipeptidase A/metabolism , Perciformes , Protein Hydrolysates/economics , Protein Hydrolysates/metabolism , Protein Hydrolysates/pharmacology , Protein Stability , Proteolysis , Spain , Subtilisin/metabolism , Trypsin/metabolism
2.
Food Funct ; 6(8): 2646-52, 2015 Aug.
Article in English | MEDLINE | ID: mdl-26134634

ABSTRACT

The aim of this work was to seasonally characterize the nutritional quality of oil extracted from small-spotted catshark (Scyliorhinus canicula) and bogue (Boops boops). The proximate composition, lipid profile and regiodistribution of the fatty acid in the glycerol backbone were analyzed. In addition, three nutritional indexes were calculated (atherogenicity and thrombogenicity indexes and the hypocholesterolaemic/hypercholesterolaemic ratio). Both species presented PUFA as the predominant fraction, the most abundant being DHA. Healthy values of the aforementioned indexes were maintained throughout the year. Moreover, the relative composition of omega 3 fatty acids at the sn-2 position ranged from 47.3 to 66.8 mol%, attracting interest in the employment of these oils as the raw source for the production of 2-monoacylglycerols. Regarding the individual behavior of each fatty acid, DHA presented a high tendency to occupy the sn-2 bond, whereas EPA presented the opposite behavior.


Subject(s)
Fatty Acids/chemistry , Fish Oils/chemistry , Perciformes/metabolism , Sharks/metabolism , Animals , Fatty Acids/isolation & purification , Fatty Acids/metabolism , Fish Oils/isolation & purification , Fish Oils/metabolism , Seasons , Stereoisomerism
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