The parameters temperature, relative humidity (RH), reaction time, mixing ratio of dextran to chicken myofibrillar proteins (Mfs), and pH were examined using random-centroid optimization, resulting in 15 vertices. After evaluating individual vertices, the optimal preparatory conditions showing the highest solubility were determined as temperature, 53℃; RH, 65%; reaction time, 47.93 h, dextran to Mfs mixing ratio, 14.4 (w/w), and pH 8.5, resulting in a 56.4 ± 10.0% solubility of the Mfs in low ionic strength medium. Sodium dodecyl sulfate-poly-acrylamide gel electrophoresis of the proteins showed decreased mobility of myosin heavy chain, suggesting the formation of dextran-conjugated Mfs. The hydroxy radical scavenging capacity of the protein was 6.3 ± 0.2 μmol of gallic acid equivalent per gram of protein. Thus, these results indicate that dextran-glycation improves the solubility of chicken Mfs in low ionic strength medium, allowing the proteins to exhibit their antioxidant activity.