Open AccessCrystallization and preliminary X‐ray study of a family 10 alkali‐thermostable xylanase from alkalophilic Bacillus sp. strain NG‐27
Author(s) -
Manikandan K.,
Bhardwaj Amit,
Ghosh Amit,
Reddy V. S.,
Ramakumar S.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105020518
Subject(s) - xylanase , hemicellulose , chemistry , hydrolysis , alkali metal , crystallization , strain (injury) , food science , biochemistry , stereochemistry , enzyme , biology , organic chemistry , anatomy
Xylanases (EC 3.2.1.8) catalyze the hydrolysis of β‐1,4‐glycosidic linkages within xylan, a major hemicellulose component in the biosphere. The extracellular endoxylanase (XylnA) from the alkalophilic Bacillus sp. strain NG‐27 belongs to family 10 of the glycoside hydrolases. It is active at 343 K and pH 8.4. Moreover, it has attractive features from the point of view of utilization in the paper pulp, animal feed and baking industries since it is an alkali‐thermostable protein. In this study, XylnA was purified from the native host source and crystallized by the hanging‐drop vapour‐diffusion method. The crystals belong to the monoclinic space group C 2, with unit‐cell parameters a = 174.5, b = 54.7, c = 131.5 Å, β = 131.2°, and diffract to better than 2.2 Å resolution.