Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases
Dilokpimol, Adiphol; Verkerk, Bart; Li, Xinxin; Bellemare, Annie; Lavallee, Mathieu; Frommhagen, Matthias; Underlin, Emilie Nørmølle; Kabel, Mirjam A.; Powlowski, Justin; Tsang, Adrian; de Vries, Ronald P.
(2022) FEBS Letters, volume 596, issue 15, pp. 1932 - 1943
(Article)
Abstract
Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards
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model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.
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Keywords: acetyl xylan esterase, carbohydrate esterase family 1, feruloyl esterase, fungi, hydroxycinnamic acid, plant biomass, Biophysics, Structural Biology, Biochemistry, Molecular Biology, Genetics, Cell Biology
ISSN: 0014-5793
Publisher: Wiley-Blackwell
Note: Funding Information: This work was supported by Genome Canada and Génome Québec. This work was partly supported by the China Scholarship Council to XL (grant no: 201803250066). The funding sources had no role in study design, in the collection, analysis and interpretation of data, in the writing of the manuscript, nor in the decision to submit the article for publication. Publisher Copyright: © 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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