Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 by Biochemical Characterization of Esterases From Uncharacterized Branches
| Autor: | Li, Xinxin, Griffin, Kelli, Langeveld, Sandra, Frommhagen, Matthias, Underlin, Emilie N., Kabel, Mirjam A., de Vries, Ronald P., Dilokpimol, Adiphol, Sub Molecular Plant Physiology, Molecular Plant Physiology |
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| Přispěvatelé: | Sub Molecular Plant Physiology, Molecular Plant Physiology, Westerdijk Fungal Biodiversity Institute - Fungal Physiology, Westerdijk Fungal Biodiversity Institute |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
CAZy Histology acetyl xylan esterase lcsh:Biotechnology Biomedical Engineering Bioengineering 02 engineering and technology Esterase Pichia pastoris plant biomass degradation Ferulic acid 03 medical and health sciences chemistry.chemical_compound Feruloyl esterase lcsh:TP248.13-248.65 Arabinoxylan Levensmiddelenchemie feruloyl esterase Original Research VLAG chemistry.chemical_classification biology Food Chemistry Chemistry carbohydrate esterase Bioengineering and Biotechnology food and beverages CAZy subfamilies 021001 nanoscience & nanotechnology biology.organism_classification 030104 developmental biology Enzyme Biochemistry Xylanase fungi 0210 nano-technology Biotechnology ferulic acid |
| Zdroj: | Frontiers in Bioengineering and Biotechnology 8 (2020) Frontiers in Bioengineering and Biotechnology, Vol 8 (2020) Frontiers in Bioengineering and Biotechnology, 8. Frontiers Media S.A. Li, X, Griffin, K, Langeveld, S, Frommhagen, M, Underlin, E N, Kabel, M A, de Vries, R P & Dilokpimol, A 2020, ' Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 by Biochemical Characterization of Esterases From Uncharacterized Branches ', Frontiers in Bioengineering and Biotechnology, vol. 8, 694 . https://doi.org/10.3389/fbioe.2020.00694 Frontiers in bioengineering and biotechnology, 8. Frontiers Media SA Frontiers in Bioengineering and Biotechnology, 8 Frontiers in Bioengineering and Biotechnology |
| ISSN: | 2296-4185 |
| DOI: | 10.3389/fbioe.2020.00694 |
| Popis: | The fungal members of Carbohydrate Esterase family 1 (CE1) from the CAZy database include both acetyl xylan esterases (AXEs) and feruloyl esterases (FAEs). AXEs and FAEs are essential auxiliary enzymes to unlock the full potential of feedstock. They are being used in many biotechnology applications including food and feed, pulp and paper, and biomass valorization. AXEs catalyze the hydrolysis of acetyl group from xylan, while FAEs release ferulic and other hydroxycinnamic acids from xylan and pectin. Previously, we reported a phylogenetic analysis for the fungal members of CE1, establishing five subfamilies (CE1_SF1–SF5). Currently, the characterized AXEs are in the subfamily CE1_SF1, whereas CE1_SF2 contains mainly characterized FAEs. These two subfamilies are more related to each other than to the other subfamilies and are predicted to have evolved from a common ancestor, but target substrates with a different molecular structure. In this study, four ascomycete enzymes from CE1_SF1 and SF2 were heterologously produced in Pichia pastoris and characterized with respect to their biochemical properties and substrate preference toward different model and plant biomass substrates. The selected enzymes from CE1_SF1 only exhibited AXE activity, whereas the one from CE1_SF2 possessed dual FAE/AXE activity. This dual activity enzyme also showed broad substrate specificity toward model substrates for FAE activity and efficiently released both acetic acid and ferulic acid (∼50%) from wheat arabinoxylan and wheat bran which was pre-treated with a commercial xylanase. These fungal AXEs and FAEs also showed promising biochemical properties, e.g., high stability over a wide pH range and retaining more than 80% of their residual activity at pH 6.0–9.0. These newly characterized fungal AXEs and FAEs from CE1 have high potential for biotechnological applications. In particular as an additional ingredient for enzyme cocktails to remove the ester-linked decorations which enables access for the backbone degrading enzymes. Among these novel enzymes, the dual FAE/AXE activity enzyme also supports the evolutionary relationship of CE1_SF1 and SF2. |
| Databáze: | OpenAIRE |
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