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Crystallization and preliminary X-ray crystallographic analysis of a putative feruloyl esterase fromTalaromyces cellulolyticus

Crystallization and preliminary X-ray crystallographic analysis of a putative feruloyl esterase fromTalaromyces cellulolyticus
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 ofTalaromyces cellulolyticus(formerly known asAcremonium 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 Mimidazole pH 8.0, 0.2 Mcalcium 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 parametersa= 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 Å3 Da−1and a solvent content of 50.88%(v/v).
Talaromyces, Crystallization, Crystallography, X-Ray, Carboxylic Ester Hydrolases
Talaromyces, Crystallization, Crystallography, X-Ray, Carboxylic Ester Hydrolases
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