SwePub
Sök i LIBRIS databas

  Utökad sökning

onr:"swepub:oai:research.chalmers.se:bdb346ee-a749-4ff1-a881-06e2c2df0592"
 

Sökning: onr:"swepub:oai:research.chalmers.se:bdb346ee-a749-4ff1-a881-06e2c2df0592" > Biochemical and str...

Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion

Arnling Bååth, Jenny, 1987 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
Mazurkewich, Scott, 1982 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
Knudsen, Rasmus Meland (författare)
Köpenhamns universitet,University of Copenhagen
visa fler...
Poulsen, Jens-Christian N (författare)
Köpenhamns universitet,University of Copenhagen
Olsson, Lisbeth, 1963 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
Lo Leggio, Leila (författare)
Köpenhamns universitet,University of Copenhagen
Larsbrink, Johan, 1982 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
visa färre...
 (creator_code:org_t)
2018-08-01
2018
Engelska.
Ingår i: Biotechnology for Biofuels. - : Springer Science and Business Media LLC. - 1754-6834 .- 1754-6834. ; 11:1
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Background Lignocellulose is highly recalcitrant to enzymatic deconstruction, where the recalcitrance primarily results from chemical linkages between lignin and carbohydrates. Glucuronoyl esterases (GEs) from carbohydrate esterase family 15 (CE15) have been suggested to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan. However, only a limited number of GEs have been biochemically characterized and structurally determined to date, limiting our understanding of these enzymes and their potential exploration. Results Ten CE15 enzymes from three bacterial species, sharing as little as 20% sequence identity, were characterized on a range of model substrates; two protein structures were solved, and insights into their regulation and biological roles were gained through gene expression analysis and enzymatic assays on complex biomass. Several enzymes with higher catalytic efficiencies on a wider range of model substrates than previously characterized fungal GEs were identified. Similarities and differences regarding substrate specificity between the investigated GEs were observed and putatively linked to their positioning in the CE15 phylogenetic tree. The bacterial GEs were able to utilize substrates lacking 4-OH methyl substitutions, known to be important for fungal enzymes. In addition, certain bacterial GEs were able to efficiently cleave esters of galacturonate, a functionality not previously described within the family. The two solved structures revealed similar overall folds to known structures, but also indicated active site regions allowing for more promiscuous substrate specificities. The gene expression analysis demonstrated that bacterial GE-encoding genes were differentially expressed as response to different carbon sources. Further, improved enzymatic saccharification of milled corn cob by a commercial lignocellulolytic enzyme cocktail when supplemented with GEs showcased their synergistic potential with other enzyme types on native biomass. Conclusions Bacterial GEs exhibit much larger diversity than fungal counterparts. In this study, we significantly expanded the existing knowledge on CE15 with the in-depth characterization of ten bacterial GEs broadly spanning the phylogenetic tree, and also presented two novel enzyme structures. Variations in transcriptional responses of CE15-encoding genes under different growth conditions suggest nonredundant functions for enzymes found in species with multiple CE15 genes and further illuminate the importance of GEs in native lignin–carbohydrate disassembly.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Mikrobiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Microbiology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Strukturbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Structural Biology (hsv//eng)

Nyckelord

Glucuronoyl esterase
Biomass conversion
Xylan
CE15
Carbohydrate-active enzyme
Carbohydrate esterase
Lignin–carbohydrate complexes

Publikations- och innehållstyp

art (ämneskategori)
ref (ämneskategori)

Hitta via bibliotek

Till lärosätets databas

Sök utanför SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy