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Crystallization and preliminary X‐ray crystallographic analysis of a putative feruloyl esterase from Talaromyces cellulolyticus
Author(s) -
Watanabe Masahiro,
Ishikawa Kazuhiko
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14024650
Subject(s) - chemistry , orthorhombic crystal system , crystallization , crystal structure , hydrolysis , stereochemistry , molecule , crystallography , biochemistry , organic chemistry
Feruloyl esterase (FAE; EC 3.1.1.73) catalyzes the cleavage of the ester bond between ferulic acid and polysaccharides in plant cell walls, and thus holds significant potential for the industrial utilization of biomass saccharification. A feruloyl esterase was identified from the genome database of Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus ). The gene consists of the catalytic domain and a carbohydrate‐binding module connected through a serine/threonine‐rich linker region. The recombinant enzyme was prepared, purified and crystallized at 293 K using 0.1 M imidazole pH 8.0, 0.2 M calcium acetate, 14% PEG 8000 as the precipitant. The crystal diffracted to 2.6 Å resolution and the crystal system is primitive orthorhombic, with unit‐cell parameters a = 90.9, b = 123.4, c = 135.4 Å. Four molecules are assumed to be present per asymmetric unit, corresponding to a Matthews coefficient of 2.50 Å 3 Da −1 and a solvent content of 50.88%( v / v ).