Characterization, functionality and antioxidant activity of water-soluble proteins extracted from bombyx mori linn.

Abstract

The yield of water-soluble protein extracted from silkworm pupae, Bombyx mori Linn. (WSPB) was 3.96% by wet weight basis. The major amino acids found in WSPB were glutamic acid, which was the most abundant, followed by histidine, phenylalanine and glycine in that order. The electrophoretic study revealed that proteins with MW of 37, 64 and 75 kDa were the major protein components in WSPB. Based on FTIR analysis, WSPB remained its structural integrity. The surface hydrophobicity, free and total sulfhydryl group contents were 3.52, 22.17 µmol/g and 23.08 µmol/g, respectively. WSPB was highly solubilized in the pH range of 5-11. WSPB exhibited poor emulsifying properties and foaming capacity but the foam stability was comparable to bovine serum albumin (BSA). WSPB had high antioxidant potential, based on DPPH • , ABTS •+ and FRAP assay. Therefore, protein from silkworm pupae is a potential source of antioxidant and can be served as an ingredient in processed foods to enhance its desired functionality and nutritional value.