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- W2007822012 abstract "Ginkgo biloba seed proteins were hydrolyzed using alkali protease and pepsin to obtain antioxidant peptides. Ginkgo biloba antioxidant peptides (GKAPs) were separated by Sephadex G-25 and Sephadex G-10 gel filtration chromatography. The GKAP B3 exhibited highest antioxidant activity. B3 peptide was separated by reversed-phase high-performance liquid chromatography (RP-HPLC), and 2 peptides with good antioxidant activity, i.e., GKAPs C8 and C9, were obtained. The molecular weight and amino acid sequences of the peptides were identified by Liquid chromatography quadrupole time-of-flight mass spectrometry (LC-Q-TOF-MS). The results showed that the molecular mass of GKAP C8 was 452.21 Da and the amino acid sequence was YVGD (Tyr-Val-Gly-Asp), while the molecular mass of GKAP C9 was 988.49 Da and the amino acid sequence was LGNTDYAVH (Leu-Gly-Asn-Thr-Asp-Tyr-Ala-Val-His). GKAPs C8 and C9 exhibited good free radical-scavenging effect and inhibited the autoxidation of the linoleic acid system." @default.
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- W2007822012 date "2013-01-01" @default.
- W2007822012 modified "2023-09-26" @default.
- W2007822012 title "Purification and Identification of Novel Antioxidant Peptides from Enzymatic Hydrolysate of Ginkgo biloba Seed Proteins" @default.
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- W2007822012 doi "https://doi.org/10.3136/fstr.19.1029" @default.
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