In this paper, the superoxide dismutase fromMartianus dermestoidesis purified by the following methods: heat treatment, polyethylene concentration, Sephadex G-75 gel filtration, and DEAE-Sepharose FF ion exchange chromatography. The result shows that the purification multiple is 3.86, the activation yield is 21.89% and the specific activation of the enzyme is 447.6 U/mg. The purified SOD appears to be a sole protein on SDS-PAGE and the molecular weight is estimated to be 40.58 kDa. H2O2can obviously inhibit the enzyme activation and CHCl3-CH3CH2OH only demonstrates basically no inhibitory effect. The type of the dermestoides SOD might be Cu/Zn-SOD. After purification, some enzymatic characterizations of the SOD are studied. The optimum reaction temperature of purified SOD is 50°C. The optimum reaction pH value of purification is 6. The dermestoide SOD has a preferable stability below 50°C and at pH values between 5-8.
Dyes are usually difficult to be decolorized due to their complex chemical structures. In this work, laccase was purified from the white rot fungus Cerrena unicolor to evaluate its application in dye decolorization. SDS-PAGE analysis showed the purified laccase to be a monomeric protein of 63.7 kDa. The optimum pH for the oxidation of 2,2-azinobis-(3-ethylbenzthiaoline-6-sufonic acid) (ABTS) was 2.2 and the optimum temperature was 50°C. The activity of the purified enzyme was strongly inhibited by sodium azide and partially inhibited by cysteine, dithiothreitol. The Km values of the purified laccase for the substrate ABTS, syringaldazine and 2,6-dimethoxyphenol were 0.217, 0.306 and 0.199 mmol/L.
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