In recent years, many advances have been made in improving the biocatalytic activities of enzymes. Interaction of enzymes and macromolecules have important role in stabilization of enzyme’s structure and function. Lysozyme lyses the bacterial cell wall by splitting ß (1–4) linkages between N-acetylmuramic acid and N-acetylglucosamine of the peptidoglycan in bacterial cell walls. Tragacanth is a polysaccharide obtained from exudates of the species of Astragalus. It is a very complex heterogeneous anionic polysaccharide of high molecular weight. Tragacanth consists of two main fractions: a water-insoluble component called bassorin, and a water-soluble component called tragacanthin. The aim of this investigation was to attach tragacanthin (water-soluble component of tragacanth) to lysozyme by Maillard reaction. The covalent attachment of this hydrocolloid with lysozyme was confirmed by SDS-PAGE and ion exchange chromatography. The conjugates exhibited improved solubility, foaming and emulsion properties. In addition, thermal stability of lysozyme in this conjugate was increased significantly. According to these results, attachment of lysozyme to tragacanthin can increase the application of this hydrocolloid as a functional component and lysozyme as a natural antimicrobial component in food and pharmaceutical industry.