Soft food gels are of high interest for food innovation that can cater to the specific needs of various populations. This study explores the innovative development of soft beta-lactoglobulin (β-LG) gels through a green process that combines heat treatment and transglutaminase (TGase)-catalyzed crosslinking at a moderate pH. The optimal procedure involves heating β-LG solutions, pH 7.5 at 80 °C for 30 min to facilitate protein unfolding and aggregation, followed by TGase catalysis at 50 U TGase/g β-LG. This process produced soft and moist β-LG gels at a low concentration of 5% (w/v). The softness of β-LG gels was characterized through rheological measurements, suggesting a low storage modulus and high frequency dependence. Morphological observations of β-LG gels using TEM showed a loosely arranged network. SDS-PAGE and FTIR analyses indicated the formation of covalent disulfide bonds and isopeptide bonds in β-LG gels through the heat and TGase treatments. The potential of the novel β-LG gels as traditional agar gel substitutes was comparatively analyzed on their textural properties. Both gels showed distinctive jelly-like characteristics, whereas β-LG gels exhibited superior softness and reduced brittleness, positioning them as viable protein-based alternatives to agar gels for various applications in both food and nonfood sectors.