Repositori URV

Identificador: imarina:6386647

Handle: https://hdl.handle.net/20.500.11797/imarina6386647

Autors:
Gallegos-Tintoré, STorres-Fuentes, CMartínez-Ayala, ALSolorza-Feria, JAlaiz, MGirón-Calle, JVioque, J

Resum:
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. © 2011 Society of Chemical Industry.