Enzymatic hydrolysis of grape seed protein: In vitro digestibility, functional, and structural insights as effected...

This study investigated the production of grape seed protein hydrolysate by studying the influence of various enzymatic hydrolysis conditions on grape seed proteins. The hydrolysate was characterized in terms of functional, structural, antioxidant properties and in vitro digestibility. The findings revealed that enzymatic hydrolysis led to structural modifications, which enhanced the functional properties of grape seed proteins. Enzymatic hydrolysis of grape seed protein with enzyme alcalase concentration @ 4 % (v/v) and 6 h resulted in the highest degree of hydrolysis, highest antioxidant activity, emulsifying capacity and solubility, and the lowest turbidity value. Enzymatic hydrolysis treatment reduced particle size, and turbidity, while improving DPPH radical scavenging activity, solubility. FTIR analysis indicated structural and conformational changes in the protein. X-ray diffraction results demonstrated reduced crystallinity in all the grape seed protein hydrolysates. The conformational as well as structural alterations contributed to improved antioxidant properties, and in-vitro digestibility of grape seed protein hydrolysate.