Structure and function of a glycoside hydrolase family 8 endoxylanase from<i>Teredinibacter turnerae</i>

Fowler, C. Andrew; Hemsworth, G.R.; Cuskin, Fiona; Hart, Sam; Turkenburg, J.P.; Gilbert, Harry J.; Walton, Paul H.; Davies, G.J.

doi:10.1107/s2059798318009737

Cited by 11 publications

(11 citation statements)

References 53 publications

(54 reference statements)

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“…A difference in the substrate binding site of xylanases can typically change the ratio of different products and cleavage specificity depends on the GH family of xylanase 40 . The xylanase from T. turnerae 41 belongs to GH8 family cannot cleave xylooligosaccharides with less than X4, while thexylanase from P. oxalicum 37 belongs to GH11 family can efficiently degrade X4 and longer xylan oligosaccharides. The catalytic activity of NhGH11 producing smaller xylooligosaccharides can be considered as an important and valuable enzymatic property for a number of industrial applications, as resulting xylooligosaccharides can be used as food ingredients and can act as a prebiotic to maintain the intestinal function 42 .…”

Section: Resultsmentioning

confidence: 99%

High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca

Andaleeb

Ullah

Perbandt³

et al. 2020

Sci Rep

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Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products. Here we present the three-dimensional structure of a xylanase from Nectria haematococca (NhGH11) at 1.0 Å resolution and its functional properties. The atomic resolution structure provides details and insights about the complex hydrogen bonding network of the active site region and allowed a detailed comparison with homologous structures. Complementary biochemical studies showed that the xylanase can catalyze the hydrolysis of complex xylan into simple xylose aldopentose subunits of different lengths. NhGH11 can catalyze the efficient breakdown of beechwood xylan, xylan polysaccharide, and wheat arabinoxylan with turnover numbers of 1730.6 ± 318.1 min−1, 1648.2 ± 249.3 min−1 and 2410.8 ± 517.5 min−1 respectively. NhGH11 showed maximum catalytic activity at pH 6.0 and 45 °C. The mesophilic character of NhGH11 can be explained by distinct structural features in comparison to thermophilic GH11 enzymes, including the number of hydrogen bonds, side chain interactions and number of buried water molecules. The enzymatic activity of NhGH11 is not very sensitive to metal ions and chemical reagents that are typically present in associated industrial production processes. The data we present highlights the potential of NhGH11 to be applied in industrial biomass degradation processes.

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Section: Resultsmentioning

confidence: 99%

High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca

Andaleeb

Ullah

Perbandt³

et al. 2020

Sci Rep

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“…T . turnerae is a facultative intracellular endosymbiont found in wood-boring bivalves, it is cellulolytic with demonstrated cellulose degrading capability and more recently it has been found to harbour a complex array of xylan degrading enzymes and lytic polysaccharide monooxygenases [ 90 , 91 ], yet it possesses a relatively small repertoire of CAZYmes that only target woody plant biomass within its genome compared to S . degradans [ 92 ].…”

Section: Discussionmentioning

confidence: 99%

Mechanistic strategies of microbial communities regulating lignocellulose deconstruction in a UK salt marsh

et al. 2021

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Background Salt marshes are major natural repositories of sequestered organic carbon with high burial rates of organic matter, produced by highly productive native flora. Accumulated carbon predominantly exists as lignocellulose which is metabolised by communities of functionally diverse microbes. However, the organisms that orchestrate this process and the enzymatic mechanisms employed that regulate the accumulation, composition and permanence of this carbon stock are not yet known. We applied meta-exo-proteome proteomics and 16S rRNA gene profiling to study lignocellulose decomposition in situ within the surface level sediments of a natural established UK salt marsh. Results Our studies revealed a community dominated by Gammaproteobacteria, Bacteroidetes and Deltaproteobacteria that drive lignocellulose degradation in the salt marsh. We identify 42 families of lignocellulolytic bacteria of which the most active secretors of carbohydrate-active enzymes were observed to be Prolixibacteracea, Flavobacteriaceae, Cellvibrionaceae, Saccharospirillaceae, Alteromonadaceae, Vibrionaceae and Cytophagaceae. These families secreted lignocellulose-active glycoside hydrolase (GH) family enzymes GH3, GH5, GH6, GH9, GH10, GH11, GH13 and GH43 that were associated with degrading Spartina biomass. While fungi were present, we did not detect a lignocellulolytic contribution from fungi which are major contributors to terrestrial lignocellulose deconstruction. Oxidative enzymes such as laccases, peroxidases and lytic polysaccharide monooxygenases that are important for lignocellulose degradation in the terrestrial environment were present but not abundant, while a notable abundance of putative esterases (such as carbohydrate esterase family 1) associated with decoupling lignin from polysaccharides in lignocellulose was observed. Conclusions Here, we identify a diverse cohort of previously undefined bacteria that drive lignocellulose degradation in the surface sediments of the salt marsh environment and describe the enzymatic mechanisms they employ to facilitate this process. Our results increase the understanding of the microbial and molecular mechanisms that underpin carbon sequestration from lignocellulose within salt marsh surface sediments in situ and provide insights into the potential enzymatic mechanisms regulating the enrichment of polyphenolics in salt marsh sediments.

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“…3d) suggests that it is clearly an endo-acting xylanase. It shares 42% and 43% identity with two characterized GH8 endo-xylanases, Xyn8A from Bacteroides intestinalis (Hong et al 2014) and TtGH8 from Teredinibacter turnerae (Fowler et al 2018), both of which also released xylotriose as their main hydrolysis product from xylan.…”

Section: Discussionmentioning

confidence: 99%

Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries

et al. 2019

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Xylanases are in important class of industrial enzymes that are essential for the complete hydrolysis of lignocellulosic biomass into fermentable sugars. In the present study, we report the cloning of novel xylanases with interesting properties from compost metagenomics libraries. Controlled composting of lignocellulosic materials was used to enrich the microbial population in lignocellulolytic organisms. DNA extracted from the compost samples was used to construct metagenomics libraries, which were screened for xylanase activity. In total, 40 clones exhibiting xylanase activity were identified and the thermostability of the discovered xylanases was assayed directly from the library clones. Five genes, including one belonging to the more rare family GH8, were selected for subcloning and the enzymes were expressed in recombinant form in E. coli . Preliminary characterization of the metagenome-derived xylanases revealed interesting properties of the novel enzymes, such as high thermostability and specific activity, and differences in hydrolysis profiles. One enzyme was found to perform better than a standard Trichoderma reesei xylanase in the hydrolysis of lignocellulose at elevated temperatures.

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Structure and function of a glycoside hydrolase family 8 endoxylanase fromTeredinibacter turnerae

Abstract: The symbionts of marine shipworms provide a rich reservoir of potential carbohydrate-active enzymes. Here, the 1.5 Å resolution three-dimensional structure of a T. turnerae GH8 xylanase is revealed and its potential in biomass degradation is highlighted.

Cited by 11 publications

References 53 publications

High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca

High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca

Mechanistic strategies of microbial communities regulating lignocellulose deconstruction in a UK salt marsh

Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries

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