Isolation, Purification and Partial Characterization of Catalase from Chinese Chives

The present study was conducted to obtain high-purity catalase(CAT) from Chinese chives and explore some of its enzymological properties.Electrophoresis-purity CAT was obtained sequentially after homogenization,extraction,frac-tional ammonium sulfate precipitation,DEAE-Sepharose chromatographic separation and Superdex-200 gel filtration.In the process,a purification factor of 70.36,a recovery of 18.33% and a specific enzyme activity of 22064.57 U/mg were obtained.The enzyme exhibited a molecular weight of 241.76 kD and contained a 62.43 kD subunite.The optimum temperature and pH for this enzyme were 37 ℃ and 7.2,respectively.The CAT enzyme was stable under pH 5-9 and 25-40 ℃ conditions.Its Km was determined to be 46.93 mmol/L under optimum conditions.The enzyme activity could be strongly inhibited by methanol,ethanol,isopropanol,SDS,Cu2+,Ag+,and Fe2+.