Sub-100-nm nanoparticles were prepared from beta-lactoglobulin (BLG) with a narrow size distribution by a desolvation method using glutaraldehyde for cross-linking. With pre-heating of the BLG solution to 60 degrees C and subsequent pH readjustment to 9.0, nanoparticles of 59 +/- 5nm were obtained with improved uniformity. Bovine serum albumin (BSA) nanoparticles, prepared under similar conditions for comparison, were larger and less uniform. The half-width of 80% particle distribution was used to compare the uniformity of particle size distribution. The stability of the nanoparticles was investigated by degradation tests at neutral and acidic pHs with and without proteolytic enzymes, trypsin and pepsin. The degradation time, determined by a graphical approach, was used to compare the relative stabilities of BLG and BSA nanoparticles. The particles of BLG were more stable than those of BSA in acidic and neutral media with and without added enzymes.