Keyword search (4,163 papers available)

"Hilden KS" Authored Publications:

Title Authors PubMed ID
1 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
2 Penicillium subrubescens adapts its enzyme production to the composition of plant biomass. Dilokpimol A, Peng M, Di Falco M, Chin A Woeng T, Hegi RMW, Granchi Z, Tsang A, Hildén KS, Mäkelä MR, de Vries RP 32408196
CSFG
3 Closely related fungi employ diverse enzymatic strategies to degrade plant biomass. Benoit I, Culleton H, Zhou M, DiFalco M, Aguilar-Osorio G, Battaglia E, Bouzid O, Brouwer CPJM, El-Bushari HBO, Coutinho PM, Gruben BS, Hildén KS, Houbraken J, Barboza LAJ, Levasseur A, Majoor E, Mäkelä MR, Narang HM, Trejo-Aguilar B, van den Brink J, vanKuyk PA, Wiebenga A, McKie V, McCleary B, Tsang A, Henrissat B, de Vries RP 26236396
CSFG
4 Comparative genomics reveals high biological diversity and specific adaptations in the industrially and medically important fungal genus Aspergillus. de Vries RP, Riley R, Wiebenga A, Aguilar-Osorio G, Amillis S, Uchima CA, Anderluh G, Asadollahi M, Askin M, Barry K, Battaglia E, Bayram Ö, Benocci T, Braus-Stromeyer SA, Caldana C, Cánovas D, Cerqueira GC, Chen F, Chen W, Choi C, Clum A, Dos Santos RA, Damásio AR, Diallinas G, Emri T, Fekete E, Flipphi M, Freyberg S, Gallo A, Gournas C, Habgood R, Hainaut M, Harispe ML, Henrissat B, Hildén KS, Hope R, Hossain A, Karabika E, Karaffa L, Karányi Z, Kraševec N, Kuo A, Kusch H, LaButti K, Lagendijk EL, Lapidus 28196534
NA

 

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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