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Purification and identification of antioxidant peptides from peanut protein isolate hydrolysates using UHR-Q-TOF mass spectrometer.

Food chemistry (2014-05-20)
Na Ji, Cuixia Sun, Yunxia Zhao, Liu Xiong, Qingjie Sun
ABSTRACT

Peanut protein isolate (PPI) was hydrolysed with alcalase to obtain antioxidant peptides. To purify these peptides, the peanut protein isolate hydrolysates (PPIH) were separated by ultrafiltration (MWCO=3kDa) and the obtained PPIH-II (Mw<3kDa) with higher antioxidant activity was further separated by gel filtration chromatography (Sephadex G-15). After filtration, both peptides, P1 and P4, with stronger antioxidant capacity were fractionated using preparative high performance liquid chromatography (P-HPLC). Three antioxidant peptides were finally purified from P1 and P4 using the UHR-Q-TOF mass spectrometer, and the amino acid sequences of the peptides were identified as Thr-Pro-Ala (286kDa), Ile/Leu-Pro-Ser (315kDa) and Ser-Pro (202kDa), respectively.

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