Thermal denaturation and gelation of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study

Abstract

The thermal denaturation and gelation properties of vicilin-rich protein isolates from red bean, red kidney bean and mung beans (further denoted as RPI, KPI and MPI) were investigated by differential scanning calorimetry (DSC) and dynamic oscillatory measurements. The relation between the properties of these proteins to their free sulphydryl (SH)/disulfide bond (SS) contents was also evaluated. DSC analyses showed that many DSC characteristics of major endothermic peak (corresponding to vicilin component), including its denaturation temperature ( T d), enthalpy changes (Δ H) and width at half-peak height (Δ T 1/2), significantly varied with the type of protein isolates. Furthermore, the heat-induced gelation, including onset of gelation and the development of mechanical moduli, was also dependent on the type of protein isolates. The thermal denaturation of these proteins was nearly unaffected by the presence of reducing agent dithiothreitol (DTT), while the presence of DTT weakened the gel formation. The T d of vicilin components and the mechanical moduli of corresponding formed gels were positively related to their SS contents. Additionally, the formed gels were thermo-irreversible, and heat pretreatment (carried out at temperatures higher than or close to the T d of these vicilins) could improve the gel network formation. These results confirm that vicilin-rich protein isolates from various legumes show different patterns of thermal denaturation and gelation, and these properties are to a great extent related to their SH and/or SS contents.