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Investigate of Process Parameters on Xylanase Enzyme Activity in Melanocarpus Albomyces Batch Culture

The thermal and operational inactivation of a commercial Xylanase from Melanocarpus Albomyces was studied in several buffered solutions usually employed to study the activity of this enzyme. Some previous works have been done to understand the effect of the of the buffers sample on the enzyme activity. Afterwards, data obtained at temperatures from 40 to 80 0 C at pH 7.0 were used to find activity, half life and de-activation constant. Both half time (t1/2) and deactivation constant have (Kd) significant effect of temperature and value of (Kd) increased by 2-3 times for each step of 10 0 C. The parameters of V max and Km obtained using Lineweaver-Burk plot method were 1.935 µ Mol /L min and 0.131 mol /L correspondingly. Enzyme activity was investigated with different buffers over wide range of pH (5.0-10.0) at room and optimum kinetic temperature indicates that pH 6.0 - 7.0 found highly suitable. The experimental results revealed good thermal stability, with greater stability at higher pH value for Xylanase in hemi- cellulosic reaction.