Expression, purification, crystallization and preliminary X-ray analysis of α-L-arabinofuranosidase B from Aspergillus kawachii

摘要

α-L-Arabinofuranosidase (EC 3.2.1.55) is one of the hemicellulases that cleave the glycosidic bonds between L-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystal-lization and preliminary X-ray analysis of α-L-arabinofuranosidase B from Aspergillus kawachii IFO4308 (AkAbfB), a family 54 glycoside hydrolase, is described. Recombinant AkAbfB was expressed in Escherichia coli and Pichia pastoris. The native crystals of recombinant AkAbfB produced by P. pastoris belong to the orthorhombic space group P2_12_12_1 (unit-cell parameters a = 39.5, b = 98.2, c = 144.0 A) and diffracted X-rays to a resolution of 1.82 A.