Abstract
In this study, an antioxidative peptide was obtained by hydrolyzation of mideodeok (Styela clava) flesh tissue with various proteases and purified through gel filtration chromatography and reverse phage-HPLC (RPHPLC), and then antioxidant activity was investigated using electron spin resonance (ESR) spectrometer. Among the enzymatic hydrolysates, the peptic hydrolysate exhibited the highest antioxidant activity, and a strong antioxidant peptide was purified from the hydrolysate. The peptide sequence, Leu-Trp-His-Thr-His (692.2 Da), was identified by quardruple time-of-flight electrospray ionization (QTOF ESI)-MS. This antioxidative peptide strongly scavenged peroxyl radical with the IC50 value of 39.4 μM.
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Kang, N., Ko, SC., Samarakoon, K. et al. Purification of antioxidative peptide from peptic hydrolysates of Mideodeok (Styela clava) flesh tissue. Food Sci Biotechnol 22, 541–547 (2013). https://doi.org/10.1007/s10068-013-0112-y
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DOI: https://doi.org/10.1007/s10068-013-0112-y