Abstract: The goal of the present work was to study the effects of acid treatment on the foaming properties of a soybean protein isolate (SPI) and its fractions, glycinin (11S) and β-conglycinin (7S). The structural characteristics, interfacial properties, foaming capacity and stability of the treated proteins were studied. Results from surface hydrophobicity and differential scanning calorimetry (DSC) showed that the acid treatment caused the complete denaturation of 11S and a partial denaturation of 7S. This protein unfolding affected their interfacial properties, which led to an improvement in the foaming properties of both protein fractions and isolate. Treated 7S showed the best behavior in the rearrangement process, probably due to it...
Interfacial (rheological) properties of soy glycinin were studied at different pH. At acidic and hig...
This study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attac...
key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; solubility;...
The goal of the present work was to study the effects of acid treatment on the foaming properties of...
To obtain a food ingredient composed of soybean and amaranth proteins with better functionality, the...
Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and...
Se desarrolló un método de batido —reológico para la caracterización cinética de los mecanismos prin...
When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed ...
Proteolysis of food proteins changes their conformation and often generates bioactive peptides, lead...
The effect of partial enzymatic hydrolysis of soy protein isolate (SPI) on its foaming properties is...
Soy hull soluble fractions (HSF) were obtained by acid or alkaline/acid extraction. By chemical char...
When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed ...
The objective of the work was to study the effect of dynamic high-pressure homogenization (HPH) on t...
In this work the influence of the acid pH treatment of soy protein isolate on the foaming properties...
Changes in solubility and molecular properties of protein films obtained from soy protein isolate (S...
Interfacial (rheological) properties of soy glycinin were studied at different pH. At acidic and hig...
This study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attac...
key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; solubility;...
The goal of the present work was to study the effects of acid treatment on the foaming properties of...
To obtain a food ingredient composed of soybean and amaranth proteins with better functionality, the...
Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and...
Se desarrolló un método de batido —reológico para la caracterización cinética de los mecanismos prin...
When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed ...
Proteolysis of food proteins changes their conformation and often generates bioactive peptides, lead...
The effect of partial enzymatic hydrolysis of soy protein isolate (SPI) on its foaming properties is...
Soy hull soluble fractions (HSF) were obtained by acid or alkaline/acid extraction. By chemical char...
When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed ...
The objective of the work was to study the effect of dynamic high-pressure homogenization (HPH) on t...
In this work the influence of the acid pH treatment of soy protein isolate on the foaming properties...
Changes in solubility and molecular properties of protein films obtained from soy protein isolate (S...
Interfacial (rheological) properties of soy glycinin were studied at different pH. At acidic and hig...
This study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attac...
key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; solubility;...