The kinetics and thermodynamics of denaturation of D-amino acid oxidase by sodium n-dodecyl sulphate (SDS) was studied in the presence and absence of additional amounts of flavin adenine dinucleotide (FAD) at various temperatures (310-325 K) in 0.02 M sodium pyrophosphate at pH = 8.3. The activity measurement data was gathered with thermodynamic data for further interpretation. The corresponding data shows higher stability for DAO against temperatures and potent denaturants like SDS.