Chemical lipophilization of soy protein isolates and wheat gluten

Chemical modification of soy protein isolate and wheat gluten can be used to investigate the influence of the chemical composition and the structure of the proteins on the final product properties and to adjust these properties to meet specific demands. Proteins were lipophilized by adding different levels of lauroyl chloride to aqueous protein dispersions. At optimum reaction conditions, incorporation rates of lauroyl chains to the protein were 400 and 300 µmol/g proteins for soy protein isolate and wheat gluten, respectively. The study showed that it was possible to lipophilize proteins in an aqueous medium, even with the protein significantly high in concentration.

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Bibliographic Details
Main Authors: Philippe-Roussel, Coralie, Pina, Michel, Graille, Jean
Format: article biblioteca
Language:fre
Published: Wiley
Subjects:Q02 - Traitement et conservation des produits alimentaires, biochimie, protéine végétale, isolat protéique, soja, gluten, hydrophobicité, acide gras, solution, http://aims.fao.org/aos/agrovoc/c_910, http://aims.fao.org/aos/agrovoc/c_8172, http://aims.fao.org/aos/agrovoc/c_6253, http://aims.fao.org/aos/agrovoc/c_14477, http://aims.fao.org/aos/agrovoc/c_3294, http://aims.fao.org/aos/agrovoc/c_33502, http://aims.fao.org/aos/agrovoc/c_2818, http://aims.fao.org/aos/agrovoc/c_28563,
Online Access:http://agritrop.cirad.fr/476994/
http://agritrop.cirad.fr/476994/1/ID476994.pdf
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Summary:Chemical modification of soy protein isolate and wheat gluten can be used to investigate the influence of the chemical composition and the structure of the proteins on the final product properties and to adjust these properties to meet specific demands. Proteins were lipophilized by adding different levels of lauroyl chloride to aqueous protein dispersions. At optimum reaction conditions, incorporation rates of lauroyl chains to the protein were 400 and 300 µmol/g proteins for soy protein isolate and wheat gluten, respectively. The study showed that it was possible to lipophilize proteins in an aqueous medium, even with the protein significantly high in concentration.