Phosphoesterification of soybean and peanut proteins with sodium trimetaphosphate (STMP): Changes in structure to improve functionality for food applications.

Author(s) Sánchez-Reséndiz, A.; Rodríguez-Barrientos, S.; Rodríguez-Rodríguez, J.; Barba-Dávila, B.; Serna-Saldivar, S.O.; Chuck-Hernández, C.
Journal Food Chem
Date Published 2018 Sep 15
Abstract

Soybean and peanut protein isolates underwent phosphorylation using sodium trimetaphosphate (STMP). Changes in functional properties and the influence of STMP (1, 2 or 3% w/w), pH (11.5 or 12.5), temperature (35 or 55 °C) and time (3 or 5 h) were evaluated. The highest degree of phosphorylation was achieved at 2% of STMP and pH 12.5. The best specific conditions varied according to the raw material: in soybean, 25% phosphorylation was achieved at 55 °C and 5 h whereas in peanut, 30% was reached at 35 °C and 3 h. The modified proteins showed an improved emulsifying activity (27.3% for soybean and 6.6% for peanut), whereas NSI for soybean increased more than three times and for peanut decreased by half. In vitro digestibility improved in both isolates around 1.5%. These results showed that phosphorylation with STMP of peanut and soybean proteins yielded isolates with a wide array of potential applications in food systems.

DOI 10.1016/j.foodchem.2018.04.009
ISSN 0308-8146
Citation Sánchez-Reséndiz A, Rodríguez-Barrientos S, Rodríguez-Rodríguez J, Barba-Dávila B, Serna-Saldivar SO, Chuck-Hernández C. Phosphoesterification of soybean and peanut proteins with sodium trimetaphosphate (STMP): Changes in structure to improve functionality for food applications. Food Chem. 2018;260:299-305.

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