CLONING, EXPRESSION, AND CHARACTERIZATION OF AN ALKALOPHILLIC ENDO-1,4-BETA-XYLANASE FROM PAENIBACILLUS SP. HPL-002

No-Joong Park, Hee Kyung Lim, Ha Young Song, Dal Rye Kim, Kee-In Lee, In Taek Hwang

Abstract


The biochemical properties of a purified enzyme of a new alkalophillic endo-1,4-beta-xylanase gene, KRICT PX2 (GU967374), which was isolated from Paenibacillus sp. HPL-002 (KCTC11410BP) and expressed in E. coli, were investigated. The specific activity of the purified xylanase was 51.26 μmol/min/mg proteins. The Km and Vmax values of the protein for birch wood xylan were also 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 50oC, respectively, and, the activity was stably maintained at 40oC. Most metallic salts, ethylenediamine tetra-acetic acid, 2-mercaptoethanol, phenylmethane-sulphonyl fluoride, and furfural, have no impact on the enzyme’s 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 practical applications.

Keywords


Alkalophyllic xylanase; Cloning; Expression; Paenibacillus sp. HPL-002

Full Text: PDF

Welcome to BioResources! This online, peer-reviewed journal is devoted to the science and engineering of biomaterials and chemicals from lignocellulosic sources for new end uses and new capabilities. The editors of BioResources would be very happy to assist you during the process of submitting or reviewing articles. Please note that logging in is required in order to submit or review articles. Martin A. Hubbe, (919) 513-3022, hubbe@ncsu.edu; Lucian A. Lucia, (919) 515-7707, lucian.lucia@gmail.com URLs: bioresourcesjournal.com; http://ncsu.edu/bioresources ISSN: 1930-2126