Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity

Felipe Andrés Venegas; Sanna Koutaniemi; Sandra M.J. Langeveld; Annie Bellemare; Sun Li Chong; Adiphol Dilokpimol; Michael J. Lowden; Kristiina S. Hilden; Juan Francisco Leyva-Illades; Miia R. Mäkelä; Thi Thanh My Pham; Mao Peng; Mark A. Hancock; Yun Zheng; Adrian Tsang; Maija Tenkanen; Justin Powlowski; Ronald P. de Vries

doi:10.1016/j.nbt.2022.04.003

Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity

Felipe Andrés Venegas
, Sanna Koutaniemi
, Sandra M.J. Langeveld
, Annie Bellemare
, Sun Li Chong
, Adiphol Dilokpimol
, Michael J. Lowden
, Kristiina S. Hilden
, Juan Francisco Leyva-Illades
, Miia R. Mäkelä
, Thi Thanh My Pham
, Mao Peng
, Mark A. Hancock
, Yun Zheng
, Adrian Tsang
, Maija Tenkanen^*
, Justin Powlowski
, Ronald P. de Vries

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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 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.

Original language	English
Pages (from-to)	28-38
Number of pages	11
Journal	New Biotechnology
Volume	70
DOIs	https://doi.org/10.1016/j.nbt.2022.04.003
Publication status	Published - 25 Sept 2022

Bibliographical 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

Funding

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 ).

Keywords

Acetyl esterase
CE16
Glucomannan
Substrate specificity
Xylan
Xyloglucan

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Cite this

Venegas, F. A., Koutaniemi, S., Langeveld, S. M. J., Bellemare, A., Chong, S. L., Dilokpimol, A., Lowden, M. J., Hilden, K. S., Leyva-Illades, J. F., Mäkelä, M. R., My Pham, T. T., Peng, M., Hancock, M. A., Zheng, Y., Tsang, A., Tenkanen, M., Powlowski, J., & de Vries, R. P. (2022). Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity. New Biotechnology, 70, 28-38. https://doi.org/10.1016/j.nbt.2022.04.003

@article{1c4904a235f94e6f9e26fc7107e3ae27,

title = "Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity",

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 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.",

keywords = "Acetyl esterase, CE16, Glucomannan, Substrate specificity, Xylan, Xyloglucan",

author = "Venegas, \{Felipe Andr{\'e}s\} and Sanna Koutaniemi and Langeveld, \{Sandra M.J.\} and Annie Bellemare and Chong, \{Sun Li\} and Adiphol Dilokpimol and Lowden, \{Michael J.\} and Hilden, \{Kristiina S.\} and Leyva-Illades, \{Juan Francisco\} and M{\"a}kel{\"a}, \{Miia R.\} and \{My Pham\}, \{Thi Thanh\} and Mao Peng and Hancock, \{Mark A.\} and Yun Zheng and Adrian Tsang and Maija Tenkanen and Justin Powlowski and \{de Vries\}, \{Ronald P.\}",

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: {\textcopyright} 2022 The Authors",

year = "2022",

month = sep,

day = "25",

doi = "10.1016/j.nbt.2022.04.003",

language = "English",

volume = "70",

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journal = "New Biotechnology",

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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 2022, 'Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity', New Biotechnology, vol. 70, pp. 28-38. https://doi.org/10.1016/j.nbt.2022.04.003

TY - JOUR

T1 - Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity

AU - Venegas, Felipe Andrés

AU - Koutaniemi, Sanna

AU - Langeveld, Sandra M.J.

AU - Bellemare, Annie

AU - Chong, Sun Li

AU - Dilokpimol, Adiphol

AU - Lowden, Michael J.

AU - Hilden, Kristiina S.

AU - Leyva-Illades, Juan Francisco

AU - Mäkelä, Miia R.

AU - My Pham, Thi Thanh

AU - Peng, Mao

AU - Hancock, Mark A.

AU - Zheng, Yun

AU - Tsang, Adrian

AU - Tenkanen, Maija

AU - Powlowski, Justin

AU - de Vries, Ronald P.

N1 - 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

PY - 2022/9/25

Y1 - 2022/9/25

N2 - 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.

AB - 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.

KW - Acetyl esterase

KW - CE16

KW - Glucomannan

KW - Substrate specificity

KW - Xylan

KW - Xyloglucan

UR - https://www.scopus.com/pages/publications/85129156452

U2 - 10.1016/j.nbt.2022.04.003

DO - 10.1016/j.nbt.2022.04.003

M3 - Article

C2 - 35405333

AN - SCOPUS:85129156452

SN - 1871-6784

VL - 70

SP - 28

EP - 38

JO - New Biotechnology

JF - New Biotechnology

ER -

Carbohydrate esterase family 16 contains fungal hemicellulose acetyl esterases (HAEs) with varying specificity

Abstract

Bibliographical note

Funding

Keywords

Access to Document

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