Enhanced Thermal Stabilization of Yeast <scp>d</scp> ‐Aspartate Oxidase Through Intersubunit Disulfide Bond Engineering

increased by 21.8°C compared with the wild-type enzyme. Biochemical analyses confirmed the formation of an intersubunit disulfide bond and suggest that it contributes to improved resistance to heat-induced loss of activity under the tested conditions, without compromising the enzyme's useful catalytic properties. Collectively, these results indicate that intersubunit disulfide engineering can improve the functional robustness of ChDDO under the assay conditions used, thereby supporting its practical use in DDO-based applications.