Abstract: The NADPH‐sulfite reductase from Saccharomyces cerevisiae was purified to electrophoretic homogeneity by ammonium sulfate fractionation, DEAE Sephacel, Sephacryl S‐300 and DEAE Sephadex A‐50 chromatography. Optimal pH was 7.3 and temperature 25°C. It was inhibited by IAA, PCMPS, PMSF, NEM, PCMB, cyanide and most divalent metal ions. For the ozonated mackerel surimi ground with purified reductase, the reactive SH increased from 2.29∞105 to 4.46∞105mole/g and gel strength from 256.7 to 360.5g·cm. According to SDS‐PAGE, the recovery of myosin heavy chain was observed on the ozonated mackerel surimi with addition of NADPH‐sulfite reductase.