The heating of a globular protein is known to elicit conformational changes in the protein molecules, resulting in the formation of a gel depending on the solution conditions. We have used dynamic light scattering (DLS) and small-angle neutron scattering (SANS) to investigate the phase behavior and structure evolution in heat induced gelation of Bovine Serum Albumin (BSA) protein as a function of pH and ionic strength. The gelation temperature is found to be increasing with increase in pH and decrease in ionic strength. The structure of the protein molecule remains intact very close to the gelation temperature. However, on further increase in temperature, the protein molecules form small aggregates which eventually lead to a network gel at gelation temperature. The gel structure is characterized by a mass fractal having a fractal dimension about 2.