![]() ![]() Qian ZJ, Jung WK, Kim SK (2008) Free radical scavenging activity of novel antioxidative peptide purified from hydrolysate of bullfrog skin ( Rana catesbeiana Shaw). Zhang T, Li YH, Miao M, Jiang B (2011) Purification and characterisation of a new antioxidant peptide from chickpea ( Cicer arietium L.) protein hydrolysates. Li Y, Jiang B, Zhang T, Mu W, Liu J (2008) Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). J Am Oil Chem Soc 85:521–527ĭe Avelar IGJ, Magalhaes MMM, Silva AB, Souza LL, Leitao AC, Hermes-Lima M (2004) Reevaluating the role of 1,10-phenanthroline in oxidative reactions involving ferrous ions and DNA damage. Zhang SB, Wang Z, Xu SY (2008) Antioxidant and antithrombotic activities of rapeseed peptides. Xie ZJ, Huang JR, Xu XM, Jin ZY (2008) Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate. Food Res Int 43:848–855Īluko RE, Monu E (2003) Functional and bioactive properties of quinoa seed protein hydrolysates. You S-J, Udenigwe CC, Aluko RE, Wu J (2010) Multifunctional peptides from egg white lysozyme. Landry J, Delhaye S (1992) Simplified procedure for the determination of tryptophan of foods and feedstuffs from barytic hydrolysis. Gehrke CW, Wall LL, Absheer JS, Kaiser FE, Zumwalt RW (1985) Sample preparation for chromatography of amino-acids: acid-hydrolysis of proteins. J Agric Food Chem 58:4712–4718īidlingmeyer BA, Cohen SA, Tarvin TL (1984) Rapid analysis of amino-acids using pre-column derivatization. Pownall TL, Udenigwe CC, Aluko RE (2010) Amino acid composition and antioxidant properties of pea seed ( Pisum sativum L.) enzymatic protein hydrolysate fractions. Girgih AT, Udenigwe CC, Aluko RE (2011) In vitro antioxidant properties of hemp seed ( Cannabis sativa L.) protein hydrolysate fractions. Tang CH, Wang XS, Yang XQ (2009) Enzymatic hydrolysis of hemp ( Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates. Shahidi F, Zhong Y (2010) Novel antioxidants in food quality preservation and health promotion. Lobo V, Patil A, Phatak A, Chandra N (2010) Free radicals, antioxidants and functional foods: impact on human health. Food Chem 116:277–284īouayed J, Bohn T (2010) Exogenous antioxidants-double-edged swords in cellular redox state: health beneficial effects at physiologic doses versus deleterious effects at high doses. Udenigwe CC, Lu Y-L, Han C-H, Hou W-C, Aluko RE (2009) Flaxseed protein-derived peptide fractions: antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages. In conclusion, the antioxidant activity of HPH after simulated GIT digestion is mainly influenced by the amino acid composition of some of its peptides. ![]() The elution time-dependent increased concentrations of the hydrophobic amino acids coupled with decreased levels of positively charged amino acids may have been responsible for the significantly higher ( p < 0.05) antioxidant properties observed for some of the peptide fractions when compared to the unfractionated HPH. Peptide separation resulted in higher concentration of some hydrophobic amino acids (especially proline, leucine and isoleucine) in the fractions (mainly F5 and F8) when compared to HPH. Inhibition of linoleic acid oxidation by some of the HPH peptide fractions was higher at 1 mg/ml when compared to that observed at 0.1 mg/ml peptide concentration. Glutathione (GSH), HPH and the RP-HPLC peptide fractions possessed low ferric ion reducing ability but all had strong (>60 %) metal chelating activities. Radical scavenging activities of the fractionated peptides increased as content of hydrophobic amino acids or elution time was increased, with the exception of hydroxyl radical scavenging that showed decreased trend. The peptide fractions exhibited higher oxygen radical absorbance capacity as well as scavenging of 2,2-diphenyl-1-picrylhydrazyl, superoxide and hydroxyl radicals when compared to HPH. Hemp seed protein hydrolysate (HPH) was produced through simulated gastrointestinal tract (GIT) digestion of hemp seed protein isolate followed by partial purification and separation into eight peptide fractions by reverse-phase (RP)-HPLC. ![]()
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