Abstract

Catalase is an effective biocatalyst to degrade hydrogen peroxide to water and oxygen that can serve in textile effluent treatment to remove residual H₂O₂. Thermostable catalases are needed to withstand both the high temperature and pH of textile wastewater. We have cloned the Mn-containing catalase gene ACS24898.1 from Geobacillus sp. WCH70, which originated from thermophilic organisms, and expressed it in Escherichia coli in activated form. The recombinant protein has been purified to homogeneity and identified to be a new homo-hexamer Mn-containing catalase. The native molecular mass of the catalase has been measured to be 138 kDa by size-exclusion chromatography. The new enzyme has optimum catalyzed activity at pH 9.0 and a temperature of 75 °C. It is thermostable up to 70 °C for 8 h incubation and maintains 80% and 50% activity, respectively, at 80 °C after 5 h and 90 °C after 1 h. At 75 °C and pH 9.0, the K_m is 67.26 mM for substrate H₂O₂ and the rate of reaction at H₂O₂ saturation, V_max, is 75,300 U/mg. The thermophilic and alkaline preferred properties of this new Mn-catalase are valuable features in textile wastewater treatment. View Full-Text