CHARACTERIZATION OF KRICT PX2 XYLANASE FROM THE Paenibacillus sp. HPL-002 FOR UTILIZATION OF PLANTS AS BIO-RESOURCES

A new alkalophyllic endo-1, 4-beta-xylanase gene, krict px2 (gu967374) isolated from paenibacillus sp. hpl-002 (kctc11410bp) was expressed in e. coli and the biochemical properties of the purified enzyme was investigated. the specific activity of the purified xylanase was 51.26 μmol/min/mg proteins. and also, km and vmax values of the protein for birch wood xylan were verified to have 0.061 μm and 55.3 μmol/min/mg proteins, respectively. the optimum ph and temperature for the activity of the enzyme were ph 8~9 and 50°c, respectively, and also the activity were stably maintained at 40°c. most metallic salts, ethylenediamine tetra-acetic acid, 2-mercaptoethanol, phenylmethane sulphonyl fluoride, and furfural have no impact on the enzyme activity at 1 mm. the simulated 3-d structure of this xylanase is similar to xyn10b from paenibacillus barcinonensis. further research on the degradation of different-origin xylans and enzyme production will be necessary for the practical application.