Title of article
CHARACTERIZATION OF KRICT PX2 XYLANASE FROM THE Paenibacillus sp. HPL-002 FOR UTILIZATION OF PLANTS AS BIO-RESOURCES
Author/Authors
Hwang, In-Taek Korea Research Institute of Chemical Technology, South Korea , Lim, Hee-Kyung Korea Research Institute of Chemical Technology, South Korea , Cho, Soo-Jin Korea Research Institute of Chemical Technology, South Korea , Kim, Dal-Rye Korea Research Institute of Chemical Technology, South Korea , Song, Ha-Young Korea Research Institute of Chemical Technology, South Korea , Lee, Kee-In Korea Research Institute of Chemical Technology, South Korea , Park, No-Joong Korea Research Institute of Chemical Technology, South Korea
From page
215
To page
227
Abstract
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.
Keywords
Alkalophyllic xylanase , cloning , expression , Paenibacillus sp. HPL , 002
Journal title
Pakistan Journal of Weed Science Research
Journal title
Pakistan Journal of Weed Science Research
Record number
2587521
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