author(s)
Priyadharshini Pachiappan, Swathiga G, Thangamalar A, Prabhu S and Mohanraj P

abstract
Sericin is a silk protein produced by the silkworm, Bombyx mori along with fibroin protein and it is removed during reeling process. The present study investigated the antioxidant properties of sericin. The ability of sericin to scavenge DPPH, superoxide, catalase and glutathione reductase was evaluated. The results indicated better anti-oxidant activity of sericin in comparison to ascorbic acid, a known anti-oxidant. The IC50 value of sericin for DPPH radical scavenging activity was found to be 0.0741 mg; whereas for ascorbic acid, it was found to be 0.213 mg. The IC50 value of sericin was found to be 0.0779, 0.0733 and 0.0701 mg for superoxide dismutase, catalase and glutathione reductase respectively. The IC50 value of ascorbic acid was found to be in the range of 0.201 to 0.226 mg. These observations indicated that sericin is able to mimic these antioxidant enzymes at very low concentration in comparison to ascorbic acid. Hence, from this study it is revealed that sericin was proved to be a better anti-oxidant in the tested parameters.