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Tryptophan residues in hyaluronidase (HAase) were modified by N-bromosuccinimide (NBS), the results indicated that there were eleven tryptophan residues in HAase, one of which was exposed and essential for the activity of the enzyme. The study on fluorescence quenching showed that KI could not quench all of the fluorescence from Trp residues in HAase, while acrylamide (Act) could quench almost all of the fluorescence from Trp residues in HAase. The collisional quenching constants (KD) of HAase at different concentrations of Act were calculated in terms of Stcm-Volmer equation. The results implied that some of the Trp residues were buried in the interior of HAase and the Trp residue on the surface of HAase was not located in the hydrophobic pocket.