High pressure processing is able to tenderize not only meat but also intramuscular connective tissue, which is mainly composed of collagen. Decorin, one of the proteoglycans, binds to and stabilizes collagen fibrils. It has been suggested that structural weakening of intramuscular connective tissue may result from the disappearance of the decorin-collagen interaction. In this study, the fluorescence spectra and the surface hydrophobicity of decorin molecules were measured under high pressure in order to examine the resulting change in the tertiary structure. The fluorescence intensity and the surface hydrophobicity of decorin molecules both decreased with increasing applied pressure and with applied time at the constant applied pressure, respectively. The observations indicate that the native structure of decorin is maintained during 200 MPa pressurization for less than 30 min.