Hydrolysis of Salmon Muscle Proteins by an Enzyme Mixture Extracted From Atlantic Salmon (Salmo Salar) Pyloric Caeca

An extract of serine proteases from thepyloric caeca of Atlantic salmon (Salmo salar) was recovered by (NH4)2SO4 and stabilized in 20% gfycerol. Proteolytic activity was determined using Azocoll and hydrofytic efficiency evaluated on salmon muscle mince. Activity assays identified chymotrypsin as the most active serine protease component, followed by trypsin and elastase. The caeca extract more efficiently hydrolyzed a salmon muscle mince substrate at 40C compared to 21.5C, and was very efficient compared to four commercial protease preparations in terms of degrees of hydrolysis (DH) achieved after a 180 min reaction. Salmon protein hydrotysates made from the enzymatic hydrolysis with the pyloric caeca enzymes had different peptide profiles at the same DH when the reaction took place at 2I.5C compared to 40C, suggesting that relative activities of these serine proteases may be different at different reaction temperatures.