Purification and Characterization of a β-Mannanase from Lactobacillus plantarum (ATCC® 14917TM)

Abstract

Mannanase alkaline was purified from thermo Lactobacillus plantarum (ATCC^® 14917^TM) 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 %.