Collagen is one of the most useful biomaterials. The medical application of collagen tissues requires specific fixation procedures. Dye-mediated photooxidation is a method of the new collagen crosslink formation. In this study, the influence of sorbitol on the extent of porcine pericardial collagen crosslinking was investigated. The collagen modification was estimated on the basis of pericardial susceptibility to pepsin digestion. The hydrolysate components were characterized electrophoretically. The significant collagen crosslinking was found in all photooxidized samples, in comparison with the untreated ones. However, the most enhanced collagen modification was observed for pericardium photooxidized with 0,5% and 0,9% sorbitol, as compared to the samples fixed without sorbitol.