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Phosphoesterification of soybean and peanut proteins with sodium trimetaphosphate (STMP): Changes in structure to

Aidee Sánchez-Reséndiz¹, Sayra Rodríguez-Barrientos², José Rodríguez-Rodríguez¹

¹Tecnologico de Monterrey, Escuela de Ingeniería y Ciencias, Monterrey, N.L., Mexico.

|April 28, 2018

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.

Keywords:

Chemical phosphorylation Functional properties Isolates Peanut Proteins Soybean

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