Thermodynamic approach to the comparative analysis of integral hydrophobicity of legumin and legumin‐T in native and denaturated forms. 1. Broad bean legumin

Abstract

The specific integral hydrophobicity of denatured forms of legumin and legumin-T from broad beans was evaluated through their hydration heat capacities. These were calculated as differences between partial heat capacities obtained from differential scanning microcalorimetry data and heat capacities in the gas phase, which were calculated by the use of the method of additive group contributions, taking into account the expansion of protein molecule in the gas phase. It is shown that there is no significant difference between the data for denatured forms of both proteins. The comparative evaluation of the hydration heat capacities of native forms of legumin and legumin-T was carried out. It is shown that the native legumin-T has a greater value of the hydration heat capacity and respectively is more hydrophobic than the native legumin. On the basis of the values of differences between the heat capacities in denatured and native states it is shown that the accessible hydrophobic surface of the native legumin-T related to a mean amino acid residue is 8-13 A* greater than that of the native legumin.

Comparative effects of limited tryptic hydrolysis on physicochemical and structural features of seed 11S globulins

“…T-derivatives of both legumins and glycinin were prepared according to a method developed earlier for broad bean legumin-T [14]. Concentrated trypsin solution was added to a 1% (w/w) protein solution in 0.05 M phosphate buffer containing 0.15 M NaCl, pH 7.6, providing for an E/S ratio 1/1000 (w/w).…”