CHARACTERIZATION AND CATALYTIC PROPERTY OF XYLAN DEGRADING ENZYME FROM MICROBIAL SOURCE

摘要

Objective: To study the catalytic property and characterization of xylan degrading enzyme from microbial source. Xylan degrading enzyme xylanase are extracted, purified and characterized from Bacillus megaterium SV1. Methods: The enzyme was purified to homogeneity by ammonium sulphate precipitation, gel permeation and ion exchange chromatographic techniques. Results: During the series of steps, 28.5 fold purification was obtained with 72.7Uper mg specific activity of xylanse and the corresponding molecular weight of the enzyme was identified as 24kDa. The optimum conditions for maximal enzyme activity were identified at pH8.0, temperature 40degreeC and with 5 of sodium chloride. It is observed that the reactants like calcium chloride_, Dithiothreitol, beetamercaptoethanol wasfound to enhance the activity of enzyme and Mercuric chloride strongly inhibits the enzyme activity. Conclusion: Degradation of Brich wood Xylan was investigated to determine the kinetic parameters Km and Vmax values and was found to be 6.1mg per ml and 280micromol per minper mg respectively. It is also verified that the enzyme Xylanase extracted from Bacillus SV1 was identified as alkalophilic and halotolerant.