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Bacterial glucuronoyl esterases can aid degradation of lignocellulose

 

Lignocellulose is highly resistant to enzymatic breakdown because of the chemical linkages between lignin, celluloses and hemicelluloses, which render enzymatic cleavage sites not accessible to hydrolases. Glucuronoyl esterases (GEs) from carbohydrate esterase family 15 (CE15) can reduce lignocellulose resistance to enzymatic attack by cleaving covalent ester bonds between lignin and glucuronoxylan.

Since there has been a need to identify new GEs that could aid lignocellulose breakdown, Arnling Bååth and colleagues (2018) characterized ten new bacterial glucuronoyl esterases. The enzymes were isolated from anaerobic Opitutus terrae, and aerobic species Spirosoma linguale and Solibacter usitatus.

Bacterial GEs were assayed on a range of model substrates from Carbosynth to test for the kinetic properties and substrate preferences of these esterases (Table 1). 

 

Product code

Substrate

Synonym

MB07246

Benzyl D-glucuronate

BnzGlcA

MA04470

Allyl D-glucuronate

AllylGlcA

MG16795

D-glucuronic acid methyl ester

MeGlcA

MG04019

D-galacturonic methyl ester

MeGalA

MT05643

1,2,3,4-tetra-O-acetyl-β-D-xylopyranose

TetAcXyl

MP03545

Poly-D-galacturonic acid methyl ester

Pectin

Table 1. List of enzyme substrates from Carbosynth used in this study.

 

The enzymatic assays showed that bacterial CE15 enzymes display lower Km values than fungal variants. Most of the bacterial enzymes tested exhibited minimal discrimination between benzyl, allyl and methyl groups on glucuronate moieties, which makes them suitable for the use on complex lignin-cellulose substrates.

For more details, read the original paper published in Biotechnology for Biofuels: Arnling Bååth et al., 2018.

 

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