Computational study of glycosaminoglycan ligands coupling with bovine testicular hyaluronidase was performed. We found displacement of hyaluronan trimers from molecular enzyme surface by chondroitin sulfate trimers. We also observed lower affinity of heparin trimers compared to other ligands (trimers of chondroitin or chondroitin sulfate). An importance of previously determined sequence of preferential binding of glycosaminoglycan ligands to hyaluronidase is emphasized. We also justified the prospects of such ligands for potential experimental study of biocatalyst structure stabilization (by chondroitin or chondroitin sulfate trimers due to non-covalent electrostatic interactions). The possibility of productive covalent modification of enzyme with chondroitin sulfate trimers for obtaining new forms of stabilized enzyme derivatives is demonstrated.