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

Neha Gupta,Nidhi Srivastava,Sameer S Bhagyawant,Gabriel Agbor

doi:10.1371/journal.pone.0191265

Neha Gupta, Nidhi Srivastava + Show 2 more

Open Access

https://doi.org/10.1371/journal.pone.0191265

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Journal: PloS one	Publication Date: Feb 6, 2018
Citations: 50	License type: CC BY 4.0

Affiliation: Jiwaji University, Banasthali University

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.

Highlights

Cardiovascular diseases (CVDs) are recognized as major causes of fatalities and presently account for 30% of human mortality [1, 2]
Vicilin was purified employing ammonium sulfate fractionation and ion exchange chromatography (Fig 1). It was present in the supernatant and further removal of minor storage proteins was achieved using dialysis where globulins were selectively precipitated while albumins remain solubilized
Mungbean vicilin consist of four subunits with molecular weights of 66.2, 45.0, 35 and 25 kDa on SDS-PAGE (Fig 2)

Summary

Introduction

Cardiovascular diseases (CVDs) are recognized as major causes of fatalities and presently account for 30% of human mortality [1, 2]. Improving food habits and life style are perceived as the suitable strategies to alleviate CVD. It necessitates the development of nutraceuticals to address these concerns [1]. The nutraceuticals are known to exert several beneficial effects on the human physiology in many ways. The edible vegetative food proteins are major sources of essential amino acids and energy for growth and development of the human body.

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