000			01987 am a22002293u 4500
042			_adc
100	1	0	_aAmengual, Neus Gacias _eauthor _91428
700	1	0	_aCsarman, Florian _eauthor
700	1	0	_aWohlschlager, Lena _eauthor _91430
700	1	0	_aLudwig, Roland _eauthor
245	0	0	_aExpression and Characterization of a Family 45 Glycosylhydrolase from Fomitopsis pinicola and comparison to Phanerochaete chrysosporium Cel45A
260			_c2022-05-01.
500			_a/pmc/articles/PMC7613719/
500			_a/pubmed/35123123
520			_aTo efficiently decompose biomass, fungi have developed various enzymatic and non-enzymatic strategies and are a source of versatile biocatalysts. The endoglucanases in glycosyl hydrolase CAZy family 45 (GH45) are known for their small size, a high thermostability and a broad substrate specificity that has been employed in textile and detergent industries. Here we report the heterologous expression and characterisation of an GH45 endoglucanase from the brown rot Fomitopsis pinicola and its direct comparison to an already characterised GH45 from the white rot Phanerochaete chrysosporium. Both enzymes were recombinantly expressed in Pichia pastoris and purified by two chromatographic steps. The biochemical characterisation highlighted the acidophilic character, with an optimal pH of 4, and a preference for amorphous substrates as carboxymethyl cellulose (CMC) and substrates containing β-1,4-glucans rather than the previously reported β-1,3/1,4-glucans lichenan and β-glucan. The dominating products from β-1,4-glucans were C3-C6 oligosaccharides, whereas from β-1,3/1,4-glucans glucose was the main reaction product. From the characterisation no differences between the brown rot and the white rot GH45 was evident.
540			_a
546			_aen
690			_aArticle
655	7		_aText _2local
786	0		_nEnzyme Microb Technol
856	4	1	_uhttp://dx.doi.org/10.1016/j.enzmictec.2022.110000 _zConnect to this object online.
999			_c1939 _d1939