Abstract
J. curcas seed proteins were fractioned according to the Osborne method and some biochemical properties were determined for these fractions. Glutelins (378 g kg–1 protein) and globulins (201 g kg –1 protein) were the main components. Albumins and prolamins were the minor components. Protein digestibility was highest in glutelins and globulins with values of 81 and 80% respectively. Electrophoresis analysis showed that globulins and glutelins exhibited similar polypeptide profiles. Electrophoresis patterns suggested that there could be a structural relationship among 2 S, 7 S and 11 S storage proteins from plant sources. According to the FAO⁄WHO reference, the protein fractions had acceptable levels of most of the essential amino acids, but its globulins and glutelins were low in lysine and tryptophan.
Highlights
J. curcas, a member of the Euphorbiaceae family, is a drought resistant multipurpose small tree of significant economic importance because of its various industrial and medical uses (Makkar et al, 2008)
The toxicity of J. curcas seed meal is ascribed to phorbol esters, non toxic genotypes which do not contain phorbol esters have been reported solely in Mexico, where kernels are consumed by humans after roasting (Makkar et al, 2008)
The protein fractionation of defatted J. curcas flour showed that glutelins and globulins are the main protein fractions in the seeds, followed by albumins and prolamins
Summary
J. curcas, a member of the Euphorbiaceae family, is a drought resistant multipurpose small tree of significant economic importance because of its various industrial and medical uses (Makkar et al, 2008). The seeds of the physic nut are a good source of oil (60% content), which could be used as a diesel substitute. They are used in medicine, soap and in cosmetic manufacturing in various tropical countries. The seed meal after the extraction of oils is rich in protein, but might be toxic to rats, mice and ruminants and it may not be suitable to be used as animal feed (Martínez et al, 2006). J. curcas seems to be a promising source of nutrients and medical compounds; the aim of this investigation was to study the chemical composition and nutritional properties of the protein fractions which remain largely unexplored
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