Application | Comment | Organism |
---|---|---|
biofuel production | efficient and complete enzymatic degradation is an essential prerequisite in the utilization of lignocellulosic material for production of energy and value-added biorefinery products. Glucuronoyl esterase CE15 is a candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment | Cerrena unicolor |
additional information | glucuronoyl esterases are highly important enzymes for industrial applications that aim for selective lignin recovery in order to obtain a final high-quality lignin product from hardwood | Cerrena unicolor |
Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme CuGE in Pichia pastoris | Cerrena unicolor |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cerrena unicolor | A0A0A7EQR3 | - |
- |
Cerrena unicolor | A0A0A7EQR3 | Daedalea unicolor | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme CuGE from Pichia pastoris by nickel affinity chromatography and ultrafiltration | Cerrena unicolor |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenylacetate + H2O | acetylxylan esterase activity | Cerrena unicolor | 4-nitrophenol + acetic acid | - |
? | |
benzyl-D-glucuronate + H2O | - |
Cerrena unicolor | benzyl alcohol + D-glucuronic acid | - |
? | |
additional information | the enzyme catalyze removal of all glucuronoxylan associated with lignin. This is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages | Cerrena unicolor | ? | - |
? | |
additional information | a lignin-enriched substrate is prepared from raw birchwood by thermal ethanol extraction, the generated lignin-rich precipitate (LRP) serves as substrate for CuGE. The chemical composition of LRP and raw birchwood is determined by acid hydrolysis and confirmes an enrichment of glucuronoyl substituted xylan and lignin with practically no structural glucan in comparison to the raw birchwood substrate. CuGE catalyzes the release of a mixture of acetylated aldouronic acids upon reaction on LRP. The enzyme shows no endoxylanase or acetyl xylan esterase activity. Glucuronoyl esterases are capable of hydrolyzing ester-linked LCCs of glucuronoxylan and lignin. LC-MS analysis shows that the product profiles contain a mixture of acetylated aldouronic acids containing 4-O-methyl-glucuronosyl (MeGlcA) ranging from DP 3 to DP 5. Substrate specificity, detailed overview | Cerrena unicolor | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
4-O-methyl-glucuronoyl methylesterase | UniProt | Cerrena unicolor |
CuGE | - |
Cerrena unicolor |
glucuronoyl esterase | - |
Cerrena unicolor |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
assay at | Cerrena unicolor |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7.5 | assay at | Cerrena unicolor |
General Information | Comment | Organism |
---|---|---|
physiological function | a natural catalytic function of CuGE glucuronoyl esterase lays in hydrolysis of genuine lignin-carbohydrate complexes from birch. The detailed product profile of aldouronic acids released from birchwood lignin by a glucuronoyl esterase from the white-rot fungus Cerrena unicolor (CuGE): CuGE releases substrate for GH10 endo-xylanase which results in significantly increased product release compared to the action of endo-xylanase alone. CuGE also releases neutral xylo-oligosaccharides that can be ascribed to the enzymes feruloyl esterase side activity as demonstrated by release of ferulic acid from insoluble wheat arabinoxylan | Cerrena unicolor |