A novel GH30 xylobiohydrolase from Acremonium alcalophilum releasing xylobiose from the non-reducing end

Šuchová, Katarína; Puchart, Vladimı́r; Spodsberg, Nikolaj; Krogh, Kristian B. R. M.; Biely, Peter

doi:10.1016/j.enzmictec.2019.109484

Cited by 28 publications

(35 citation statements)

References 37 publications

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“…Rho was better substrate than GX for AaXyn30A and TrXynIV and equally good for HcXyn30A. Xylobiohydrolases AaXyn30A and HcXyn30A were shown to cleave also β-1,3-linkages which may contribute to better hydrolysis of Rho [14,17]. The lower extent of Rho and AraX hydrolysis by TlXyn30A in comparison to GX also supports the hypothesis that MeGlcA substitution is somehow recognized by TlXyn30A, but its presence is not crucial for the enzyme activity.…”

Section: Discussionsupporting

confidence: 54%

“…On the other hand, activities of HcXyn30A, AaXyn30A and TrXynIV on all three substrates were comparable (except of TrXynIV acting on GXR), indicating that the MeGlcA carboxyl group does not play a significant role in the substrate recognition. It is in consonance with a predominant exo-action of these three enzymes [14,16,17]. In the case of TlXyn30A, the activity on GXE and GXR was approximately three times lower than on GX.…”

Section: Activity Of Gh30 Xylanases On 4-o-methylglucuronoxylan and Its Derivativessupporting

confidence: 56%

“…Bacterial enzymes from Clostridium acetobutylicum CaXyn30A (Ca) and Hungateiclostridium clariflavum HcXyn30A (Hc) are not specialized for the hydrolysis of GX, but they represent nonspecific xylanase and xylobiohydrolase, respectively [10,14]. Fungal GH30-7 xylanases tested were glucuronoxylanase TrXynVI from Trichoderma reesei (TrVI), reducing-end xylose releasing xylanase/endoxylanase TrXynIV from T. reesei (TrIV), xylobiohydrolase/endoxylanase AaXyn30A from Acremonium alcalophilum (Aa) and a nonspecific xylanase TlXyn30A from Talaromyces leycettanus (Tl) [15][16][17][18][19]. As expected, specific activity of the glucuronoxylanases EcXyn30A, BsXynC, RcXyn30A, CtXyn30A, and TrXynVI on GXE and GXR were considerably lower than that on GX (Figure 1), confirming that these enzymes require free carboxyl group of the uronic acid residue for their action.…”

Section: Activity Of Gh30 Xylanases On 4-o-methylglucuronoxylan and Its Derivativesmentioning

confidence: 99%

“…β-Xylosidase was a recombinant Aspergillus niger enzyme from GH3 family expressed in Saccharomyces cerevisiae [33]. Enzymes EcXyn30A (42 kDa), BsXynC (44 kDa), TrXynIV (43 kDa), TrXynVI (57 kDa), TlXyn30A (55 kDa), AaXyn30A (58 kDa) were prepared as described previously [5,[15][16][17][18]34]. CtXyn30A (54 kDa) (product number: CZ0445) was purchased from NZYTech, HcXyn30A (58 kDa) (product number: CZ0916) and RcXyn30A (48 kDa) (product number: CZ10281) were a generous gift of Prof. Carlos M.G.A.…”

Section: Substrates Standards and Enzymesmentioning

confidence: 99%

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Catalytic Diversity of GH30 Xylanases

et al. 2021

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Catalytic properties of GH30 xylanases belonging to subfamilies 7 and 8 were compared on glucuronoxylan, modified glucuronoxylans, arabinoxylan, rhodymenan, and xylotetraose. Most of the tested bacterial GH30-8 enzymes are specific glucuronoxylanases (EC 3.2.1.136) requiring for action the presence of free carboxyl group of MeGlcA side residues. These enzymes were not active on arabinoxylan, rhodymenan and xylotetraose, and conversion of MeGlcA to its methyl ester or its reduction to MeGlc led to a remarkable drop in their specific activity. However, some GH30-8 members are nonspecific xylanases effectively hydrolyzing all tested substrates. In terms of catalytic activities, the GH30-7 subfamily is much more diverse. In addition to specific glucuronoxylanases, the GH30-7 subfamily contains nonspecific endoxylanases and predominantly exo-acting enzymes. The activity of GH30-7 specific glucuronoxylanases also depend on the presence of the MeGlcA carboxyl, but not so strictly as in bacterial enzymes. The modification of the carboxyl group of glucuronoxylan had only weak effect on the action of predominantly exo-acting enzymes, as well as nonspecific xylanases. Rhodymenan and xylotetraose were the best substrates for exo-acting enzymes, while arabinoxylan represented hardly degradable substrate for almost all tested GH30-7 enzymes. The results expand current knowledge on the catalytic properties of this relatively novel group of xylanases.

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Section: Discussionsupporting

confidence: 54%

Section: Activity Of Gh30 Xylanases On 4-o-methylglucuronoxylan and Its Derivativessupporting

confidence: 56%

Section: Activity Of Gh30 Xylanases On 4-o-methylglucuronoxylan and Its Derivativesmentioning

confidence: 99%

Section: Substrates Standards and Enzymesmentioning

confidence: 99%

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Catalytic Diversity of GH30 Xylanases

et al. 2021

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“…In addition, some glycoside hydrolases such as GH30 xylanase and GH26 mannase secreted by T. harzianum EM0925 have been rarely studied in Trichoderma. Synergy between cellulolytic enzymes and these enzymes from Acremonium alcalophilum and Aspergillus nidulans has been described, which deserves more attention in the future [48,49]. The currently reported lignocellulosic degrading bacteria and fungi with industrial application prospects presented distinct optimal conditions for different enzymes even in the same induced enzyme system, and the stabilities against temperature and pH were also different, so it is necessary to determine the optimal conditions for enzymatic hydrolysis and saccharification with overall consideration [1,50,51].…”

Section: Discussionmentioning

confidence: 99%

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Zhang

Yang

Luo

et al. 2020

IJMS

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Fermentable sugars are important intermediate products in the conversion of lignocellulosic biomass to biofuels and other value-added bio-products. The main bottlenecks limiting the production of fermentable sugars from lignocellulosic biomass are the high cost and the low saccharification efficiency of degradation enzymes. Herein, we report the secretome of Trichoderma harzianum EM0925 under induction of lignocellulose. Numerously and quantitatively balanced cellulases and hemicellulases, especially high levels of glycosidases, could be secreted by T. harzianum EM0925. Compared with the commercial enzyme preparations, the T. harzianum EM0925 enzyme cocktail presented significantly higher lignocellulolytic enzyme activities and hydrolysis efficiency against lignocellulosic biomass. Moreover, 100% yields of glucose and xylose were obtained simultaneously from ultrafine grinding and alkali pretreated corn stover. These findings demonstrate a natural cellulases and hemicellulases mixture for complete conversion of biomass polysaccharide, suggesting T. harzianum EM0925 enzymes have great potential for industrial applications.

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The first crystal structure of a xylobiose‐bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10

et al. 2022

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Xylobiose is a prebiotic sugar that has applications in functional foods. This report describes the first X-ray crystallographic structure models of apo and xylobiose-bound forms of a xylobiohydrolase (XBH) from Acetivibrio clariflavus. This xylan-active enzyme, a member of the recently described glycoside hydrolase family 30 (GH30), subfamily 10, phylogenetic clade has been shown to strictly release xylobiose as its primary hydrolysis product. Inspection of the apo structure reveals a glycone region X 2 -binding slot. When X 2 binds, the non-reducing xylose in the À2 subsite is highly coordinated with numerous hydrogen bond contacts while contacts in the À1 subsite mostly reflect interactions typical for GH30 and enzymes in clan A of the carbohydrate-active enzymes database (CAZy). This structure provides an explanation for the high functional specificity of this new bacterial GH30 XBH subfamily.

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A novel GH30 xylobiohydrolase from Acremonium alcalophilum releasing xylobiose from the non-reducing end

Cited by 28 publications

References 37 publications

Catalytic Diversity of GH30 Xylanases

Catalytic Diversity of GH30 Xylanases

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

The first crystal structure of a xylobiose‐bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10

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