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Bellamya bengalensis, an edible mollusca, serves as a protein rich food source for the tribes in India. The objective of the present study was to isolate the protein fraction of the edible foot part of B. bengalensis for hydrolysis with three proteases, namely papain, pepsin, and alcalase. B. bengalensis protein isolates and hydrolysates were characterised for the functional properties like protein solubility index, emulsifying property, foaming property. The proximate composition of the protein isolate was determined along with nutritional value that included biological value, protein efficiency ratio, amino acid score, nutritional index, essential amino acid index. The molecular weight distribution of the protein isolate and the three hydrolysates were analyzed by SDS-PAGE. The hydrolysates were fractionated by ultrafiltration and the in vitro antioxidative properties were measured. The antihypertensive property of the in vitro angiotensin converting enzyme inhibitory activity of the hydrolysates was compared with the standard drug lisinopril. Thus, the results indicated that the hydrolyzed peptides had potent antioxidative and antihypertensive activity. The enzyme pepsin and papain produced partially hydrolyzed peptides suitable for use in the bakery industry while alcalase hydrolysis resulted in shorter peptides with the antihypertensive activity that may be used as a promising nutraceutical.

Enzymatically excised oligopeptides from Bellamya bengalensis shows potent antioxidative and anti-hypertensive activity