Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

Santos, C.R.; Costa, P.A.C.R.; Vieira, P.S.; Gonzalez, Sinkler E. T.; Corrêa, Thamy Lívia Ribeiro; Lima, E.A.; Mandelli, F; Pirolla, Renan Augusto Siqueira; Domingues, M.N.; Cabral, Lucélia; Martins, Marcele Pandeló; Cordeiro, R.L.; Junior, Atílio T; Souza, B.P.; Prates, Érica T.; Gozzo, Fábio C.; Persinoti, Gabriela Félix; Skaf, Munir S.; Murakami, Mário Tyago

doi:10.1038/s41589-020-0554-5

Cited by 27 publications

(37 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Protein expression and purification were conducted as reported in Santos et al 69 . Briefly, E. coli BL21 strain was transformed with target genes subcloned into the pET28a vector in frame to a 6×His-Tag at the N-terminus.…”

Section: Methodsmentioning

confidence: 99%

Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides

et al. 2022

Self Cite

View full text Add to dashboard Cite

The largest living rodent, capybara, can efficiently depolymerize and utilize lignocellulosic biomass through microbial symbiotic mechanisms yet elusive. Herein, we elucidate the microbial community composition, enzymatic systems and metabolic pathways involved in the conversion of dietary fibers into short-chain fatty acids, a main energy source for the host. In this microbiota, the unconventional enzymatic machinery from Fibrobacteres seems to drive cellulose degradation, whereas a diverse set of carbohydrate-active enzymes from Bacteroidetes, organized in polysaccharide utilization loci, are accounted to tackle complex hemicelluloses typically found in gramineous and aquatic plants. Exploring the genetic potential of this community, we discover a glycoside hydrolase family of β-galactosidases (named as GH173), and a carbohydrate-binding module family (named as CBM89) involved in xylan binding that establishes an unprecedented three-dimensional fold among associated modules to carbohydrate-active enzymes. Together, these results demonstrate how the capybara gut microbiota orchestrates the depolymerization and utilization of plant fibers, representing an untapped reservoir of enzymatic mechanisms to overcome the lignocellulose recalcitrance, a central challenge toward a sustainable and bio-based economy.

show abstract

Section: Methodsmentioning

confidence: 99%

Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides

et al. 2022

Self Cite

View full text Add to dashboard Cite

show abstract

“…Although the endo-β-1,3-glucanases of many glycoside hydrolase families can hydrolyze various β-1,3-glucan substrates, their catalytic modes and three-dimensional structures are sometimes very different. The fundamental and assorted roles of β-1,3-glucans in nature demand sophisticated and intricate β-1,3-glucan degrading enzymatic systems for their processing . The three-dimensional structures of different glycoside hydrolase families endo-β-1,3-glucanases demonstrate six typical folding structures: (1) GH-A (β/α) 8 TIM-barrel (GH5, GH17, GH128, GH157, and GH158); (2) GH-B β-jelly roll (GH16); (3) parallel β-helix (GH55); (4) crescent-like fold (GH64); (5) (α/α)6 barrel (GH81); and (6) thaumatin-like β-jelly roll (GH152) (Supporting Information, Figure S5).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Glycoside Hydrolase Family 157 Endo-β-1,3-Glucanase That Displays Antifungal Activity against Phytopathogens

Qin

Zhang

et al. 2023

J. Agric. Food Chem.

View full text Add to dashboard Cite

β-1,3-Glucan-degrading enzymes are widely used in fields such as food processing, plant protection, and breweries. In this work, we identified a glycoside hydrolase (GH) family 157 endo-β-1,3-glucanase (BsGlc157A) from Bacteroides sp. M27 and characterized its biochemical properties, structural model, and antifungal activity. Enzymological characterization indicated that BsGlc157A performs its optimal catalytic activity at pH 6.0 and 40 °C. BsGlc157A adopted the classic (β/α) 8 TIM-barrel structure. Two catalytic residues, the nucleophile (Glu215) and the proton donor (Glu123), were confirmed via structural modeling and sitedirected mutagenesis. Moreover, BsGlc157A hydrolyzed curdlan into a series of oligosaccharides with polymerization degrees 2−5 and exhibited inhibitory effects on the hyphal growth of typical fruit pathogenic fungi (Monilinia fructicola, Alternaria alternata, and Colletotrichum gloeosporioides), thereby illustrating effective biocontrol activity. These results revealed the catalytic properties and the application potential of GH family 157 β-1,3-glucanase, thus providing valuable biochemistry information about the group of carbohydrate-active enzymes.

show abstract

“…Protein expression and puri cation were conducted as reported in (73). Brie y, E. coli BL21 strain was transformed with target genes subcloned into pET28a in frame to a 6xHisTag at N-terminus.…”

Section: Protein Expression and Puri Cationmentioning

confidence: 99%

Gut Microbiome of the Amazon Master of the Grasses Harbors Unprecedented Enzymatic Strategies for Plant Glycans Breakdown

Cabral

Persinoti

Paixao

et al. 2020

Preprint

Self Cite

View full text Add to dashboard Cite

BackgroundPlant biomass is a promising feedstock to replace fossil-based products including fuels, chemicals and materials. However, the high resistance of plant biomass to either physicochemical or biological deconstruction has been hampering its broad industrial utilization and, consequently, the transition to a sustainable bioeconomy. The gut system from herbivores are formidable bioreactors in nature for lignocellulose breakdown and the diverse ecological niches where herbivores are found have led to the rise of a myriad of molecular strategies to cope with the sheer complexity of plant polysaccharides. This study illuminates how the unexplored microbiota of the largest living rodent, capybara, found in Pantanal wetlands and the Amazon basin, can efficiently depolymerize and utilize lignocellulosic biomass. ResultsHere, we have elucidated the gut microbial structure and composition of the semiaquatic herbivorous capybara through multi-omics approaches. Metabolic reconstruction of this microbiota showed that cellulose degradation is chiefly performed by Fibrobacter bacteria, whereas hemicelluloses and pectins are processed by a broad arsenal of Carbohydrate-Active enZymes (CAZymes) organized in polysaccharide utilization loci (PULs) identified in multiple metagenome-assembled genomes from the phylum Bacteroidetes. Furthermore, metabolomics analysis showed short chain fatty acids as major fermentation products, which are key markers of digestion performance of plant polysaccharides. Exploring the genomic dark matter of this gut microbial community, two novel CAZymes families were unveiled including a glycoside hydrolase family of β-galactosidases and a carbohydrate-binding module family involved in xylan binding that establishes an unprecedented three-dimensional fold among associated modules to CAZymes. ConclusionsOur results unveil how the capybara gut microbiota orchestrates the depolymerization and utilization of dietary plant polysaccharides, representing an untapped reservoir of new and intricate enzymatic strategies to overcome the recalcitrance of plant polysaccharides, a central challenge toward a circular and sustainable economy.

show abstract

Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

Cited by 27 publications

References 60 publications

Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides

Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides

Characterization of a Glycoside Hydrolase Family 157 Endo-β-1,3-Glucanase That Displays Antifungal Activity against Phytopathogens

Gut Microbiome of the Amazon Master of the Grasses Harbors Unprecedented Enzymatic Strategies for Plant Glycans Breakdown

Contact Info

Product

Resources

About