Amino acid composition and antioxidant properties of pea seed ( Pisum sativum L.) enzymatic protein hydrolysate fractions.
The amino acid composition and antioxidant activities of peptide fractions obtained from HPLC separation of a pea protein hydrolysate (PPH) were studied. Thermolysin hydrolysis of pea protein isolate and ultrafiltration (3 kDa molecular weight cutoff membrane) yielded a PPH that was separated into five fractions (F1-F5) on a C(18) reverse phase HPLC column. The fractions that eluted later from the column (F3-F5) contained higher contents hydrophobic and aromatic amino acids when compared to fractions that eluted early or the original PPH. Fractions F3-F5 also exhibited the strongest radical scavenging and metal chelating activities; however, hydrophobic character did not seem to contribute to reducing power of the peptides. In comparison to glutathione, the peptide fractions had significantly higher (p < 0.05) ability to inhibit linoleic acid oxidation and chelate metals. In contrast, glutathione had significantly higher (p < 0.05) free radical scavenging properties than the peptide fractions.
Pownall
Trisha L
TL
Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T2N2, Canada.
Udenigwe
Chibuike C
CC
Aluko
Rotimi E
RE
D000596:Amino Acids / Q000032:analysis*; D000975:Antioxidants / Q000737:chemistry*; D006868:Hydrolysis; D018532:Pisum sativum / Q000196:embryology*; D012639:Seeds / Q000737:chemistry* / Q000201:enzymology
D000596:Amino Acids; D000975:Antioxidants