Heat induced gelation of pulse protein networks

This study examines the effect of salts (0.5 M NaCl or 0.25 M CaCl2) and protein concentration (7.5-15%) on the gel-forming abilities of lentil (LPC), yellow pea (YPC), and faba bean (FPC) protein concentrates formed at pH 7.0. The surface hydrophobicity of YPC (84.8 arbitrary units, a.u.) was found to be lower than LPC (147.2 a.u.) and FPC (135.0 a.u.). In contrast, the surface charge for LPC, YPC, and FPC was -37.8, -28.4, and -29.3 mV, respectively. The Lg/Vn ratio of YPCs was determined as 0.65 followed by LPC (0.57) and FPC (0.41). The presence of salts reduced the least gelling concentration. LPC and FPC also appeared to have a more ordered structure than YPC as evident by CLSM. The network appeared more ordered as the protein concentration increased or in the presence of NaCl or CaCl2 according to CLSM and synchrotron based micro computed tomography (mu CT).

Automated summary

This study investigated the gel-forming abilities and structures of lentil, yellow pea, and faba bean protein concentrates under the influence of salts and protein concentration. Different protein concentrates exhibited variations in gelation ability and structure, with yellow pea protein concentrate showing lower surface hydrophobicity and lentil and faba bean presenting a more ordered structure under the studied conditions.