The objective of the present study was to investigate the effects of superchilling combined with cryoprotectants (a mixture of sucrose and sorbitol, 1:1) on protein oxidation and structural changes in common carp (Cyprinus carpio) surimi. With increasing storage time, the carbonyl content of myofibrillar proteins increased from 31.4 nmol/mg of protein (0 day) to 53.4, 46.3, and 39.7 nmol/mg protein at 35 days (P < 0.05) for −1 °C superchilled, −3 °C superchilled, and −3 °C superchilled with cryoprotectants samples, respectively. The incorporation of cryoprotectants into common carp surimi was found to significantly inhibit the formation of carbonyls (P < 0.05). The protein surface hydrophobicity increased in a similar direction, and the sulfhydryl content and Ca-ATPase stability decreased (P < 0.05). Emulsifying activities, gel textural hardness, springiness, and water binding capacity were also decreased, but they exhibited significant improvements at −3 °C when combined with cryoprotectants (P < 0.05). These results suggest that superchilling treatments at −3 °C combined with cryoprotectants offer an effective approach to reducing protein oxidation in carp surimi, thereby reducing protein structural changes known to impair the texture of surimi products.