Water-based protein-surfactant gels, formed by mixing bovine serum albumin (BSA) and sodium dodecyl sulfate in water, were investigated by rheological methods. The measurements were performed for many different protein-to-surfactant ratios as a function of the applied frequency, stress, or strain, as well as by changing the temperature, in the range between 15 and 65 degrees C. The rheological behavior of the gels as a function of applied frequency is interpreted in terms of the overlapping of at least two viscoelastic relaxation processes. The rheological results indicate the presence of thermal transitions from essentially viscous to mainly elastic regimes, in analogy with the thermal gelation processes observed in polymer solutions. The thermal gelation threshold in the present system is modulated by the protein/surfactant ratio. Differential scanning calorimetry measurements were also performed to determine whether thermal gelation is somehow concomitant to protein denaturation. The results indicate that the thermal denaturation of BSA in protein-surfactant based gels occurs at slightly higher temperatures than in the bulk. Scanning electron microscopy indicates the occurrence in the gel structure of globules formed by the arrangement of fibrils.