Kabel MA

References (5)

Title : Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl\/acetyl xylan esterases - Dilokpimol_2022_FEBS.Lett__
Author(s) : Dilokpimol A , Verkerk B , Li X , Bellemare A , Lavallee M , Frommhagen M , Normolle Underlin E , Kabel MA , Powlowski J , Tsang A , de Vries RP
Ref : FEBS Letters , : , 2022
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 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. CE1_1 - AXE1B_MYCSE Axe1 MsAxe1 Corse1p7_016869 mycse-axe1b CE1_2 SF6 FAE1B_MYCSE Fxe1 CE1_5 SF5 FAE1C_MYCSE Fae1 MsFae1 Corse1p7_018453 mycse-fae1c CE1_5 SF5 FAE1E_MYCSE Fae2 MsFae2 Corse1p7_001265 mycse-fae1e Non-CE1 SF2 FAE1F_MYCSE Fae3 MsFae3 Corse1p7_018656 mycse-fae1f
ESTHER : Dilokpimol_2022_FEBS.Lett__
PubMedSearch : Dilokpimol_2022_FEBS.Lett__
PubMedID: 35187647
Gene_locus related to this paper: emeni-axe1 , aspng-a0a100iph2 , talem-e9m3d1 , myctt-g2qd29 , chatd-g0sbz2 , chatd-g0s216 , mycse-fae1c , mycse-fae1f , mycse-fae1e , mycse-axe1b , mycse-fae4 , acrth-axe1a , chagb-q2gyn8

Title : Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 by Biochemical Characterization of Esterases From Uncharacterized Branches - Li_2020_Front.Bioeng.Biotechnol_8_694
Author(s) : Li X , Griffin K , Langeveld S , Frommhagen M , Underlin EN , Kabel MA , de Vries RP , Dilokpimol A
Ref : Front Bioeng Biotechnol , 8 :694 , 2020
Abstract : 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.
ESTHER : Li_2020_Front.Bioeng.Biotechnol_8_694
PubMedSearch : Li_2020_Front.Bioeng.Biotechnol_8_694
PubMedID: 32671051

Title : Feruloyl Esterases for Biorefineries: Subfamily Classified Specificity for Natural Substrates - Underlin_2020_Front.Bioeng.Biotechnol_8_332
Author(s) : Underlin EN , Frommhagen M , Dilokpimol A , van Erven G , de Vries RP , Kabel MA
Ref : Front Bioeng Biotechnol , 8 :332 , 2020
Abstract : Feruloyl esterases (FAEs) have an important role in the enzymatic conversion of lignocellulosic biomass by decoupling plant cell wall polysaccharides and lignin. Moreover, FAEs release anti-oxidative hydroxycinnamic acids (HCAs) from biomass. As a plethora of FAE candidates were found in fungal genomes, FAE classification related to substrate specificity is an indispensability for selection of most suitable candidates. Hence, linking distinct substrate specificities to a FAE classification, such as the recently classified FAE subfamilies (SF), is a promising approach to improve the application of these enzymes for a variety of industrial applications. In total, 14 FAEs that are classified members of SF1, 5, 6, 7, 9, and 13 were tested in this research. All FAEs were investigated for their activity toward a variety of substrates: synthetic model substrates, plant cell wall-derived substrates, including lignin, and natural substrates. Released HCAs were determined using reverse phase-ultra high performance liquid chromatography coupled to UV detection and mass spectrometry. Based on this study, FAEs of SF5 and SF7 showed the highest release of FA, pCA, and diFAs over the range of substrates, while FAEs of SF6 were comparable but less pronounced for diFAs release. These results suggest that SF5 and SF7 FAEs are promising enzymes for biorefinery applications, like the production of biofuels, where a complete degradation of the plant cell wall is desired. In contrast, SF6 FAEs might be of interest for industrial applications that require a high release of only FA and pCA, which are needed as precursors for the production of biochemicals. In contrast, FAEs of SF1, 9 and 13 showed an overall low release of HCAs from plant cell wall-derived and natural substrates. The obtained results substantiate the previous SF classification as a useful tool to predict the substrate specificity of FAEs, which eases the selection of FAE candidates for industrial applications.
ESTHER : Underlin_2020_Front.Bioeng.Biotechnol_8_332
PubMedSearch : Underlin_2020_Front.Bioeng.Biotechnol_8_332
PubMedID: 32391342
Gene_locus related to this paper: stehr-ShFae1 , 9euro-a0a1l9t4i5 , aspng-AnFaeJ , 9euro-a0a1l9t9j3 , 9euro-a0a1l9txk3 , myctt-faeb , aspnc-faec , aspni-FAEA , 9euro-a0a1l9tdb5 , myctt-g2qmb4 , 9euro-g4xkn5

Title : Characterization and mode of action of two acetyl xylan esterases from Chrysosporium lucknowense C1 active towards acetylated xylans - Pouvreau_2011_Enzyme.Microb.Technol_49_312
Author(s) : Pouvreau L , Jonathan MC , Kabel MA , Hinz SW , Gruppen H , Schols HA
Ref : Enzyme Microb Technol , 49 :312 , 2011
Abstract : Two novel acetyl xylan esterases, Axe2 and Axe3, from Chrysosporium lucknowense (C1), belonging to the carbohydrate esterase families 5 and 1, respectively, were purified and biochemically characterized. Axe2 and Axe3 are able to hydrolyze acetyl groups both from simple acetylated xylo-oligosaccharides and complex non-soluble acetylglucuronoxylan. Both enzymes performed optimally at pH 7.0 and 40 degrees C. Axe2 has a clear preference for acetylated xylo-oligosaccharides (AcXOS) with a high degree of substitution and Axe3 does not show such preference. Axe3 has a preference for large AcXOS (DP 9-12) when compared to smaller AcXOS (especially DP 4-7) while for Axe2 the size of the oligomer is irrelevant. Even though there is difference in substrate affinity towards acetylated xylooligosaccharides from Eucalyptus wood, the final hydrolysis products are the same for Axe2 and Axe3: xylo-oligosaccharides containing one acetyl group located at the non-reducing xylose residue remain as examined using MALDI-TOF MS, CE-LIF and the application of an endo-xylanase (GH 10).
ESTHER : Pouvreau_2011_Enzyme.Microb.Technol_49_312
PubMedSearch : Pouvreau_2011_Enzyme.Microb.Technol_49_312
PubMedID: 22112517
Gene_locus related to this paper: thiha-g2qdy2 , myctt-g2qd29

Title : Biochemical characterization and relative expression levels of multiple carbohydrate esterases of the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate - Kabel_2011_Appl.Environ.Microbiol_77_5671
Author(s) : Kabel MA , Yeoman CJ , Han Y , Dodd D , Abbas CA , de Bont JA , Morrison M , Cann IK , Mackie RI
Ref : Applied Environmental Microbiology , 77 :5671 , 2011
Abstract : We measured expression and used biochemical characterization of multiple carbohydrate esterases by the xylanolytic rumen bacterium Prevotella ruminicola 23 grown on an ester-enriched substrate to gain insight into the carbohydrate esterase activities of this hemicellulolytic rumen bacterium. The P. ruminicola 23 genome contains 16 genes predicted to encode carbohydrate esterase activity, and based on microarray data, four of these were upregulated >2-fold at the transcriptional level during growth on an ester-enriched oligosaccharide (XOS(FA,Ac)) from corn relative to a nonesterified fraction of corn oligosaccharides (AXOS). Four of the 16 esterases (Xyn10D-Fae1A, Axe1-6A, AxeA1, and Axe7A), including the two most highly induced esterases (Xyn10D-Fae1A and Axe1-6A), were heterologously expressed in Escherichia coli, purified, and biochemically characterized. All four enzymes showed the highest activity at physiologically relevant pH (6 to 7) and temperature (30 to 40 degrees C) ranges. The P. ruminicola 23 Xyn10D-Fae1A (a carbohydrate esterase [CE] family 1 enzyme) released ferulic acid from methylferulate, wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters, but exhibited negligible activity on sugar acetates. As expected, the P. ruminicola Axe1-6A enzyme, which was predicted to possess two distinct esterase family domains (CE1 and CE6), released ferulic acid from the same substrates as Xyn10D-Fae1 and was also able to cleave O-acetyl ester bonds from various acetylated oligosaccharides (AcXOS). The P. ruminicola 23 AxeA1, which is not assigned to a CE family, and Axe7A (CE7) were found to be acetyl esterases that had activity toward a broad range of mostly nonpolymeric acetylated substrates along with AcXOS. All enzymes were inhibited by the proximal location of other side groups like 4-O-methylglucuronic acid, ferulic acid, or acetyl groups. The unique diversity of carbohydrate esterases in P. ruminicola 23 likely gives it the ability to hydrolyze substituents on the xylan backbone and enhances its capacity to efficiently degrade hemicellulose.
ESTHER : Kabel_2011_Appl.Environ.Microbiol_77_5671
PubMedSearch : Kabel_2011_Appl.Environ.Microbiol_77_5671
PubMedID: 21742923
Gene_locus related to this paper: prer2-axea1 , prer2-axfa