Antioxidant properties of Australian canola meal protein hydrolysates

被引:163
作者
Alashi, Adeola M. [1 ,2 ,4 ]
Blanchard, Christopher L. [1 ,3 ]
Mailer, Rodney J. [1 ]
Agboola, Samson O. [1 ,2 ]
Mawson, A. John [1 ,2 ]
He, Rong [4 ]
Girgih, Abraham [4 ]
Aluko, Rotimi E. [4 ]
机构
[1] Charles Sturt Univ, EH Graham Ctr Agr Innovat, Wagga, NSW 2678, Australia
[2] Charles Sturt Univ, Sch Agr & Wine Sci, Wagga, NSW 2678, Australia
[3] Charles Sturt Univ, Sch Biomed Sci, Wagga, NSW 2678, Australia
[4] Univ Manitoba, Dept Human Nutr Sci, Richardson Ctr Funct Foods & Nutraceut, Winnipeg, MB R3T 2N2, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Canola; Antioxidant properties; Protein hydrolysates; Membrane ultrafiltration; Radical scavenging activities; Trolox equivalent antioxidant capacity (TEAC); FUNCTIONAL-PROPERTIES; ENZYMATIC-HYDROLYSIS; IN-VITRO; LIPID-PEROXIDATION; RAPESEED PEPTIDES; FRACTIONS; PURIFICATION; PROTEASES; MEMBRANE; PRODUCTS;
D O I
10.1016/j.foodchem.2013.09.081
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
Antioxidant activities of canola protein hydrolysates (CPHs) and peptide fractions prepared using five proteases and ultrafiltration membranes (1, 3, 5, and 10 kDa) were investigated. CPHs had similar and adequate quantities of essential amino acids. The effective concentration that scavenged 50% (EC50) of the ABTS.(+) was greatest for the <1 kDa pancreatin fraction at 10.1 mu g/ml. CPHs and peptide fractions scavenged DPPH center dot(+) with most of the EC50 values being <1.0 mg/ml. Scavenging of superoxide radical was generally weak, except for the <1 kDa pepsin peptide fraction that had a value of 51%. All CPHs inhibited linoleic acid oxidation with greater efficiency observed for pepsin hydrolysates. The oxygen radical absorbance capacity of Alcalase, chymotrypsin and pepsin hydrolysates was found to be better than that of glutathione (GSH) (p < 0.05). These results show that CPHs have the potential to be used as bioactive ingredients in the formulation of functional foods against oxidative stress. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:500 / 506
页数:7
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