The global demand for soybean protein has increased dramatically over the last few years due to its versatility. High pressure (HP) processing is emerging as an effective alternative to thermal processing of foods. The HP treatment of protein solutions at different process conditions can cause partial unfolding of proteins that can lead to the irreversible gelation of the product. In this study, the influence of protein concentration (5-20% w/v), pH (3-7), sugar (5% w/v), CaCl2 (5% w/v), pressure level (up to 650 MPa) and holding time (0.1 and 10 min), and process temperature (20 and 40 degrees C) on the dynamic theology of soybean protein concentrate (SPC) solutions was evaluated. Furthermore, the protein structural changes caused by HP were studied, through the use of the extrinsic fluorescence of the probe 8-anilino-1-naphthalene sulfonic acid (ANS) and Fourier transform infrared (FTIR) spectroscopy. Results indicated a strong influence of protein concentration on both elastic (G') and viscous (G '') moduli, increasing with concentration. Increase in pressure and holding time produced an increase on both G' and G '' for SPC concentrations higher than 10%; at 15% SPC concentration, a relatively low pressure treatment of 250 MPa achieved the cross-over of G' over G ''. The structure of the soybean proteins suffered limited changes after HP treatment; hydrophobicity increased, as well as the relative proportion of random coil, while the beta-sheet content decreased. HP treatment can be used to enhance the viscoelastic behavior of SPC after which SPC can be used to enrich both protein content and textural properties of foods. (C) 2008 Elsevier Ltd. All rights reserved.