Characterization of Soybean Proteins–Fatty Acid Systems View Full Text


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Article Info

DATE

2009-12-11

AUTHORS

A. Quiroga, María C. Añón, María Cecilia Puppo

ABSTRACT

This study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attachment of a low chain fatty acid, decanoic acid, to alkaline and acid soybean proteins; and the effect on their conformational and functional properties. The extent of esterification was high at acid pH and also increased with heating. Protein solubility decreased, mainly at the highest temperature (60 °C). Increasing levels of fatty acid formed a complex with a slightly more soluble protein with less surface hydrophobicity. Esterified proteins exhibited aggregation/dissociation and were stabilized by different protein subunits belonging to 7S and 11S globulins. Denaturation of these soybean protein fractions (7S and 11S) were also detected in these complexes. The highest level of fatty acids favored formation of a more ordered protein structure. More... »

PAGES

507-514

References to SciGraph publications

  • 2003-06-01. Rheological properties of emulsions containing modified soy protein isolates in JOURNAL OF THE AMERICAN OIL CHEMISTS' SOCIETY
  • 1985-12-01. The structure and complexity of the 11S polypeptides in soybeans in JOURNAL OF THE AMERICAN OIL CHEMISTS' SOCIETY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11746-009-1522-0

    DOI

    http://dx.doi.org/10.1007/s11746-009-1522-0

    DIMENSIONS

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