A novel bioactive peptide derived from enzymatic hydrolysis of Ruditapes philippinarum: Purification and investigation of its free-radical quenching potential

作者：Kim Eun Kyung; Hwang Jin Woo; Kim Yon Suk; Ahn Chang Bum; Jeon You Jin; Kweon Hyuk Jung; Bahk Young Yil; Moon Sang Ho; Jeon Byong Tae; Park Pyo Jarn^*

来源：Process Biochemistry, 2013, 48(2): 325-330.

DOI：10.1016/j.procbio.2012.10.016

• Ruditapes philippinarum
• Enzymatic hydrolysis
• Antioxidant peptide
• Free radical

We purified a novel antioxidant peptide from Ruditapes philippinarum (R. philippinarum) and investigated its free radical scavenging activities. To prepare the peptide, eight proteases were tested for enzymatic hydrolysis. alpha-chymotrypsin hydrolysate, which showed clearly superior hydroxyl radical scavenging activity (p %26lt; 0.05), were further purified using a flow filtration system and consecutive chromatographic methods. Finally, a novel antioxidant peptide was obtained, and the sequence was identified as Ser-Val-Glu-Ile-Gln-Ala-Leu-Cys-Asp-Met. The peptide from R. philippinarum effectively scavenged hydroxyl, DPPH, alkyl and superoxide radicals, with observed IC50 values of 0.042, 0.091, 0.107 and 0.372 mg/ml, respectively. This is the first report of an antioxidant peptide derived from the hydrolysates of R. philippinarum which, further, possesses competitive free radical quenching potential.

• 出版日期2013-2