Conjugation of polysaccharides to proteins utilizing the Maillard reaction leads to significant improvement in the functional properties of proteins, such as solubility, emulsification, and thermal stability. However, no gelation properties of conjugates have previously been reported. In this study, we studied the conjugation reaction between sodium caseinate (NaCN) and maltodextrin100 (Md100) in aqueous solutions via the initial stage of the Maillard reaction. The rheological properties of acid-induced gels made from NaCN-Md conjugates prepared by Maillard reaction were investigated. Acidification was performed by the addition of glucono-delta-lactone at 30°C. Covalently linked conjugates of NaCN and Md100 were produced by incubating aqueous solutions containing 5% NaCN and 5% Md100 at 90°C for 10 h. The covalent attachment of Md100 to NaCN was confirmed by SDS-PAGE with both protein and carbohydrate staining. The Schiff base formation of NaCN-Md conjugates was monitored by maximum absorbance peak at ∼300 nm using UV spectroscopy. Conjugation resulted in faster gelation (higher pH) but lower storage modulus and shear stress values of acid gels compared with gel made with NaCN only. An increase of loss tangent was also observed in acid gel made with conjugates. These results indicate that conjugates modify protein gelation and a potential use for these NaCN-Md could be as specialty functional food ingredients.