Purification of a novel nitric oxide inhibitory peptide derived from enzymatic hydrolysates of Mytilus coruscus.

Abstract

Shellfish contain significant levels of high quality protein and are therefore a potential source for biofunctional high-value peptides. To purify a novel anti-inflammatory peptide from Mytilus coruscus (M. coruscus), we applied enzymatic hydrolysis and tangential flow filtration (TFF) and investigated its nitric oxide inhibitory property. To prepare the peptide, eight proteases were employed for enzymatic hydrolysis. Flavouzyme hydrolysates, which showed clearly superior nitric oxide inhibitory activity on lipopolysaccharide (LPS)-stimulated RAW264.7, were further purified using a TFF system and consecutive chromatographic methods. Finally, a novel anti-inflammatory peptide composed of 10 amino acid residues was obtained, and the sequence was identified as Gly-Val-Ser-Leu-Leu-Gln-Gln-Phe-Phe-Leu at N-terminal position. The peptide from M. coruscus effectively inhibited nitric oxide production on macrophage cells. This is the first report of an anti-inflammatory peptide derived from the hydrolysates of M. coruscus.

DOI: 10.1016/j.fsi.2013.02.023

Cite this paper

@article{Kim2013PurificationOA, title={Purification of a novel nitric oxide inhibitory peptide derived from enzymatic hydrolysates of Mytilus coruscus.}, author={Eun-kyung Kim and Yon-Suk Kim and Jin-Woo Hwang and Seo Hee Kang and Dong-Kug Choi and Kwang-Ho Lee and Jung Suck Lee and Sang-Ho Moon and Byong-Tae Jeon and Pyo-Jam Park}, journal={Fish & shellfish immunology}, year={2013}, volume={34 6}, pages={1416-20} }