Biochemical evaluation of protein fractions from physic nut (Jatropha curcas L.)

L. Peralta-Flores; S. Gallegos-Tintore; J. Solorza-Feria; G. Davila-Ortiz; L. Chel-Guerrero; A. Martinez-Ayala

doi:10.3989/gya.072511

Biochemical evaluation of protein fractions from physic nut (Jatropha curcas L.)

L. Peralta-Flores, S. Gallegos-Tintore, J. Solorza-Feria, G. Davila-Ortiz, L. Chel-Guerrero, A. Martinez-Ayala

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

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 2S, 7S and 11S 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.

Original language	English
Pages (from-to)	253-259
Number of pages	7
Journal	Grasas y Aceites
Volume	63
Issue number	3
DOIs	https://doi.org/10.3989/gya.072511
State	Published - Jul 2012

Keywords

Albumins
Globulins
Glutelins
Jatropha curcas L.
Prolamins
Storage proteins

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10.3989/gya.072511

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title = "Biochemical evaluation of protein fractions from physic nut (Jatropha curcas L.)",

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 2S, 7S and 11S 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.",

keywords = "Albumins, Globulins, Glutelins, Jatropha curcas L., Prolamins, Storage proteins",

author = "L. Peralta-Flores and S. Gallegos-Tintore and J. Solorza-Feria and G. Davila-Ortiz and L. Chel-Guerrero and A. Martinez-Ayala",

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T1 - Biochemical evaluation of protein fractions from physic nut (Jatropha curcas L.)

AU - Peralta-Flores, L.

AU - Gallegos-Tintore, S.

AU - Solorza-Feria, J.

AU - Davila-Ortiz, G.

AU - Chel-Guerrero, L.

AU - Martinez-Ayala, A.

PY - 2012/7

Y1 - 2012/7

N2 - 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 2S, 7S and 11S 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.

AB - 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 2S, 7S and 11S 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.

KW - Albumins

KW - Globulins

KW - Glutelins

KW - Jatropha curcas L.

KW - Prolamins

KW - Storage proteins

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U2 - 10.3989/gya.072511

DO - 10.3989/gya.072511

M3 - Artículo

SN - 0017-3495

VL - 63

SP - 253

EP - 259

JO - Grasas y Aceites

JF - Grasas y Aceites

IS - 3

ER -

Biochemical evaluation of protein fractions from physic nut (Jatropha curcas L.)

Abstract

Keywords

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