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Evaluation 0f Citrus aurantium Flower as a New Source of Proteases for Fish Hydrolysate Production

Mazorra MMA, Moreno HJM, Torres LMJ, Juan C. Ramírez SJC, González CAF and Cordoba BV

Proteases screening from several nontraditional plant sources is gaining relevance in research, medicine, and food processing due to their important roles in plant physiology, therapeutic and potential use in biotechnological processes. Citrus aurantium flower contains proteases in high concentration and its potential use as a new source of proteases for fish hydrolysate production was evaluated. The effect of pH (4, 7 and 9) and citrus proteases (CPs) concentration (2.5 and 5% E/S) on protein hydrolysis of tilapia muscle (Oreochromis sp.) was determined by SDSPAGE analysis. Different protein degradation patterns were observed at different pH. A non-specific higher protein degradation on fish muscle proteins was observed at pH 4, using 5.0% CPs concentration (E/S) at 50°C after 2 h of hydrolysis, generating low molecular weight (<10 kDa) peptides. At neutral pH, CPs hydrolyzed preferentially myofibrillar proteins (myosin and actin), releasing peptide fragments of approximately 31 and 10 kDa. Degradation protein pattern observed at pH 9, was less intense. The diverse degradation patterns observed for tilapia muscle protein under different hydrolysis conditions offer possibilities for the use of CPs from Citrus aurantium flower for the production of protein hydrolysates to be used as functional ingredients and/or bioactive peptides.