Keyword search (4,163 papers available)

"Bellemare A" Authored Publications:

Title Authors PubMed ID
1 Expansion of Auxiliary Activity Family 5 sequence space via biochemical characterization of six new copper radical oxidases Fong JK; Mathieu Y; Vo MT; Bellemare A; Tsang A; Brumer H; 38953370
CSFG
2 Functional screening pipeline to uncover laccase-like multicopper oxidase enzymes that transform industrial lignins Sharan AA; Bellemare A; DiFalco M; Tsang A; Vuong TV; Edwards EA; Master ER; 38000639
CSFG
3 Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation Mathieu Y; Raji O; Bellemare A; Di Falco M; Nguyen TTM; Viborg AH; Tsang A; Master E; Brumer H; 37679837
CSFG
4 Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93 Zhao H; Karppi J; Nguyen TTM; Bellemare A; Tsang A; Master E; Tenkanen M; 36476312
CSFG
5 Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity Venegas FA; Koutaniemi S; Langeveld SMJ; Bellemare A; Chong SL; Dilokpimol A; Lowden MJ; Hilden KS; Leyva-Illades JF; Mäkelä MR; My Pham TT; Peng M; Hancock MA; Zheng Y; Tsang A; Tenkanen M; Powlowski J; de Vries RP; 35405333
CSFG
6 Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases Dilokpimol A; Verkerk B; Li X; Bellemare A; Lavallee M; Frommhagen M; Nørmølle Underlin E; Kabel MA; Powlowski J; Tsang A; de Vries RP; 35187647
CSFG
7 Fungal Genomic DNA Extraction Methods for Rapid Genotyping and Genome Sequencing. Bellemare A, John T, Marqueteau S 29876805
CSFG

 

Title:Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity
Authors:Venegas FAKoutaniemi SLangeveld SMJBellemare AChong SLDilokpimol ALowden MJHilden KSLeyva-Illades JFMäkelä MRMy Pham TTPeng MHancock MAZheng YTsang ATenkanen MPowlowski Jde Vries RP
Link:https://pubmed.ncbi.nlm.nih.gov/35405333/
DOI:10.1016/j.nbt.2022.04.003
Publication:New biotechnology
Keywords:Acetyl esteraseCE16GlucomannanSubstrate specificityXylanXyloglucan
PMID:35405333 Category: Date Added:2022-04-12
Dept Affiliation: CSFG
1 Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, QC, H4B 1R6, Canada.
2 Department of Food and Nutrition, Faculty of Agriculture and Forestry, University of Helsinki, Agnes Sjöbergin katu 2, 00014, Helsinki, Finland.
3 Fungal Physiology, Westerdijk Fungal Biodiversity Institute & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584CT Utrecht, The Netherlands.
4 Department of Microbiology, Faculty of Agriculture and Forestry, University of Helsinki, Viikinkaari 9, 00014, Helsinki, Finland.
5 SPR-MS Facility, Department of Pharmacology & Therapeutics, McGill University, 3655 Prom. Sir William Osler, Montreal, QC, H3G 1Y6, Canada.
6 Department of Food and Nutrition, Faculty of Agriculture and Forestry, University of Helsinki, Agnes Sjöbergin katu 2, 00014, Helsinki, Finland. Electronic address: maija.tenkanen@helsinki.fi

Description:

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 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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