OPTIMIZATION OF ANGIOTENSIN I‐CONVERTING ENZYME INHIBITORY PEPTIDE PRODUCTION BY RIBBONFISH (TRICHIURUS HAUMELA) BACKBONE HYDROLYSIS USING RESPONSE SURFACE METHODOLOGY

摘要: The effect of an acid protease hydrolysis on protein from ribbonfish backbone to produce peptides with angiotensin I-converting enzyme inhibitory activity (ACEIP) was studied and optimized using response surface methodology (RSM). To optimize the reaction, a three-step design used which included fractional factorial design, steepest ascent central composite (CCD). results showed that optimal conditions ACEIP were: pH 2.67, temperature 45C, substrate ratio 1/150 (g/g protein), water 1:4.38 (g/mL) time period 7.0 h. With these conditions, hydrolyzate concentration (mg/mL) inhibited 50% (ACEIC50) 1.054 ± 0.016 mg/mL, compared well predicted value (1.050 mg/mL) by RSM model. PRACTICAL APPLICATIONS Ribbonfish is one principle catches China Sea. It processed into various fish products in many factories coastal areas. However, significant amounts (12% protein, wet weight) are by-products or waste processing, not fully utilized. often as animal feedstuff. This study presents use bioactive activity, through optimizing methodology.