Antioxidant and chelating activity of Jatropha curcas L. protein hydrolysates

BACKGROUND: Antioxidant and chelating activities were determined in protein hydrolysates that were produced by treating a protein isolate of a non‐toxic genotype of Jatropha curcas with the protease preparation alcalase. RESULTS: 50 min protein hydrolysate with a degree of hydrolysis of 31.7% showed highest antioxidant and chelating activity. These activities were also determined in six peptidic fractions that were separated by gel filtration chromatography of the 50 min hydrolysate. The lower‐molecular‐weight peptidic fractions had the highest antioxidant and chelating activities, which correlated with a higher content in antioxidant and chelating amino acids such as tyrosine and histidine. CONCLUSION: Results show that J. curcas represents a good source of bioactive peptides. This may be important for the revalorization of defatted J. curcas flour, a by‐product resulting form oil extraction for biodiesel production. This is especially important in Third World and developing countries such as Mexico. Copyright © 2011 Society of Chemical Industry