Protein conjugation of curdlan belonging to $eta$-1, 3-glucan was carried out to improve it surface functionalities. The glucan was mixed with phosvitin, {TEX}$$alpha$_{s}$</TEX>{/TEX}-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and he resulting powder was incubated at 6$0^{circ}C$ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. conjugation with unfolding proteins, i.e., phosvitin and {TEX}$$alpha$_{s}$</TEX>{/TEX}-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbmin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the {TEX}$$alpha$_{s}$</TEX>{/TEX}-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and {TEX}$$alpha$_{s}$</TEX>{/TEX}-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.