Evaluation of physicochemical and functional properties of cottonseed protein hydrolyzed protein by Alcalase enzyme

Bioactive peptides are organic substances composed of amino acids, which are linked by covalent bonds, are known as peptide bonds or amide bonds. Although some of these peptides are free in natural products, but many of them are encrypted in the primary protein structures that are released through enzymatic processes. The aim of this study was to evaluate the physicochemical and functional properties of hydrolyzed protein derived from cottonseed meal by alcalase enzyme. The enzyme hydrolysis was investigated with alcalase enzyme at constant pH equal to 8, different time interval (2, 3.5 and 5 hours), temperature (45, 50 and 55 °C) and enzyme/ substrate ratio (0.5, 1.5 and 2 %). Optimization of enzyme hydrolysis was performed by surface response method. In optimal conditions, some of the hydrolyzed protein features including antioxidant activity of hydrolyzed proteins derived from cottonseed meal, including free radical DPPH inhibiting, iron ion fermentation strength, capacity total antioxidants and regenerative effects were investigated. The results of this study show that with a degree of hydrolysis 32%. The optimal hydrolysis conditions for cottonseed meal protein were 5 hours, 55 °C and the ratio of enzyme to the substrate 1.7%, In these conditions, the optimum amount of free radical inhibitory activity DPPH was 62.69%, total antioxidant capacity was 2.1 mmol α-tocopherol/mL, regenerative capacity equaled 0.078%, and chelating capacity was 80.20%. The bioactive peptides derived from cottonseed meal have physicochemical and functional properties. The response surface method was also used as an easy, reliable and available method to optimize protein hydrolysis and was effective in achieving desirable health features. Therefore, the use of cottonseed hydrolyzed proteins is recommended in some of food and medicinal formulations.