Mannanase alkaline was purified from thermo Lactobacillus plantarum (ATCC® 14917TM) using ammonium sulfate precipitation and DEAE- Sephadex ion exchange chromatography and Sephacryl S200 Gel filtration chromatography techniques, in 36% yield and 111 -fold. Gel filtration chromatography and SDS-PAGE electrophoresis were executed pure enzyme systems 35 kDa and 55 kDa. Enzyme subunits were determined as two subunits. Optimum pH 10 and 40 °C was determeined at the optimum temperature. Enzyme activities were retained fairly between 30-80 oC. It was observed that purified mannanase in a wide range was mostly stable at elevated temperatures. In addition, the effects of some metal ions such as Ca2+, Mn2+, Co2+, Zn2+, Cu2+, Fe2+ and Ni2+ on mannanase enzymes activity was assayed and all the metal ions were increased the enzyme activity from 100 to 344 %.
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