Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity
Venegas, Felipe Andrés; Koutaniemi, Sanna; Langeveld, Sandra M.J.; Bellemare, Annie; Chong, Sun Li; Dilokpimol, Adiphol; Lowden, Michael J.; Hilden, Kristiina S.; Leyva-Illades, Juan Francisco; Mäkelä, Miia R.; My Pham, Thi Thanh; Peng, Mao; Hancock, Mark A.; Zheng, Yun; Tsang, Adrian; Tenkanen, Maija; Powlowski, Justin; de Vries, Ronald P.
(2022) New Biotechnology, volume 70, pp. 28 - 38
(Article)
Abstract
Acetyl esterases are an important component of the enzymatic machinery fungi use to degrade plant biomass and are classified in several Carbohydrate Esterase families of the CAZy classification system. Carbohydrate Esterase family 16 (CE16) is one of the more recently discovered CAZy families, but only a small number of its
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enzyme members have been characterized so far, revealing activity on xylan-derived oligosaccharides, as well as activity related to galactoglucomannan. The number of CE16 genes differs significantly in the genomes of filamentous fungi. In this study, four CE16 members were identified in the genome of Aspergillus niger NRRL3 and it was shown that they belong to three of the four phylogenetic Clades of CE16. Significant differences in expression profiles of the genes and substrate specificity of the enzymes were revealed, demonstrating the diversity within this family of enzymes. Detailed characterization of one of these four A. niger enzymes (HaeA) demonstrated activity on oligosaccharides obtained from acetylated glucuronoxylan, galactoglucomannan and xyloglucan, thus establishing this enzyme as a general hemicellulose acetyl esterase. Their broad substrate specificity makes these enzymes highly interesting for biotechnological applications in which deacetylation of polysaccharides is required.
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Keywords: Acetyl esterase, CE16, Glucomannan, Substrate specificity, Xylan, Xyloglucan, Biotechnology, Bioengineering, Molecular Biology
ISSN: 1871-6784
Publisher: Elsevier
Note: Funding Information: MRM and AD were supported by the European Union, Grant agreement no: 613868 (OPTIBIOCAT). AB, mL and YZ were supported by funds from Genome Canada (Canada) and Genome Quebec (Canada). FAV was supported by the “Industrial Biocatalysis Network” funded by the Natural Sciences and Engineering Research Council of Canada Strategic Network program (Canada). The McGill SPR-MS Facility thanks the Canada Foundation for Innovation (Canada) for infrastructure support (Bruker ultrafleXtremeTM MALDI-TOF/TOF system; CFI Grant #32616 ). Publisher Copyright: © 2022 The Authors
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