Vicilin—A major storage protein of mungbean exhibits antioxidative potential, antiproliferative effects and ACE inhibitory activity

Abstract

Enzymatic hydrolysates of different food proteins demonstrate health benefits. Search for diet related food protein hydrolysates is therefore of interest within the scope of functional foods. Mungbean is one of the popular foods in India because of rich protein source. In this study, mungbean vicilin protein (MBVP) was enzymatically hydrolysed by alcalase and trypsin under optimal conditions. We have studied the antioxidant, antiproliferative and angiotensin-converting enzyme (ACE) inhibitory activities of mungbean vicilin protein hydrolysate (MBVPH) vis-a-vis alcalase-generated mungbean vicilin protein hydrolysate (AMBVPH) and trypsin-generated mungbean vicilin protein hydrolysate (TMBVPH). The results showed that MBVPH exhibited higher antioxidant potential, ACE inhibitory and antiproliferative activities than MBVP. The alcalase treated hydrolysate displayed highest ACE inhibitory activity with IC50 value of 0.32 mg protein/ml. The MBVP showed significant antiproliferative activity against both MCF-7 and MDA-MB-231 breast cancer cells at the doses between 0.2–1.0 mg/ml. The data suggested that MBVPH can be utilized as physiologically active functional foods with sufficient antihypertensive activity. The results indicate that mungbean can be utilized as a rich resource of functional foods.