The aim of this work was to investigate how the heat-induced gelation of micellar casein (MC)-plant protein mixtures in aqueous solution is affected by protein composition (MC/plant proteins = 100/0 to 0/100) and total protein content (4%, 6% and 8% w/w) at pH 5.8 and 6.0. Two types of plant proteins were used: soy proteins (SP) and pea proteins (PP). Storage moduli (G′) were measured during heating ramps from 20 to 90 °C and heat-induced gelation was characterised by a sharp increase in G′ at a critical temperature (T_c). The gel stiffness (G_el) was determined after 1 h at 90 °C and the microstructure before and after heating was investigated by confocal laser scanning microscopy (CLSM). T_c was found to increase with increasing the fraction of MC replaced by SP or PP, due to binding of calcium to the plant proteins. The effect was stronger for SP, which bound calcium more efficiently than PP. T_c decreased with decreasing pH, possibly caused by decreased electrostatic repulsion and increased calcium release from MC. G_el increased with increasing total protein content and did not depend significantly on the pH. Interestingly, G_el showed a minimum as a function of the plant protein fraction (40% for SP and 70% for PP) in the mixtures. It is concluded that MC and plant proteins did not co-aggregate in the mixtures during heating, and that each type of protein formed networks independently.