Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114702,IEDB_1394182,IEDB_142488,IEDB_146664,IEDB_983930,IEDB_983931,SB_192

• Article ID: 4158
  O'Neill MA, Darvill AG, Albersheim P, Chou KJ "Structural analysis of an acidic polysaccharide secreted by Xanthobacter sp. (ATCC 53272)" - Carbohydrate Research 206 (1990) 289-296
  

  The structure of an acidic polysaccharide secreted by a Xanthobacter sp. has been investigated by glycosyl-residue and glycosyl-linkage composition analyses, and the characterization of oligoglycosyl fragments of the polysaccharide has been carried out by chemical analyses, 1H-n.m.r. spectroscopy, fast-atom bombardment mass spectrometry, and electron-impact mass spectrometry. The polysaccharide, which contains O-acetyl groups (approximately 5%) that have not been located, has the tetraglycosyl repeating unit 1 and belongs to a group of structurally related polysaccharides synthesized by both Alcaligenes and Pseudomonas species.

  NCBI PubMed ID: 2073637
  Publication DOI: 10.1016/0008-6215(90)80068-E
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: University of Georgia Complex Carbohydrate Center, Athens, USA
  Methods: gel filtration, 1H NMR, GLC-MS, FAB-MS, partial acid hydrolysis, acid hydrolysis, GLC, methanolysis
  
   
  
  Xanthobacter sp. NW11, Xanthobacter sp. ATCC 53272
  CSDB ID 116077 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 856
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42801 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 724
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42802 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 724
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42803 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 460
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114702,IEDB_115136,IEDB_140630,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42804 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 592
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42805 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 724
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42806 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 592
Compound class: glucuronoxylan
Contained glycoepitopes: IEDB_114701,IEDB_114702,IEDB_115136,IEDB_140630,IEDB_167188,IEDB_174332,IEDB_423153

• Article ID: 8542
  Martínez PM, Appeldoorn MM, Gruppen H, Kabel MA "The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides" - Biotechnology for Biofuels 9 (2016) ID 105
  

  Background: The production of biofuels and biochemicals from grass-type plant biomass requires a complete utilisation of the plant cellulose and hemicellulosic xylan via enzymatic degradation to their constituent monosaccharides. Generally, physical and/or thermochemical pretreatments are performed to enable access for the subsequent added carbohydrate-degrading enzymes. Nevertheless, partly substituted xylan structures remain after pretreatment, in particular the ones substituted with (4-O-methyl-)glucuronic acids (UAme). Hence, α-glucuronidases play an important role in the degradation of UAmexylan structures facilitating the complete utilisation of plant biomass. The characterisation of α-glucuronidases is a necessity to find the right enzymes to improve degradation of recalcitrant UAmexylan structures. Results: The mode-of-action of two α-glucuronidases was demonstrated, both obtained from the fungus Rasamsonia emersonii; one belonging to the glycoside hydrolase (GH) family 67 (ReGH67) and the other to GH115 (ReGH115). Both enzymes functioned optimal at around pH 4 and 70 °C. ReGH67 was able to release UAme from UAme-substituted xylo-oligosaccharides (UAmeXOS), but only the UAme linked to the non-reducing end xylosyl residue was cleaved. In particular, in a mixture of oligosaccharides, UAmeXOS having a degree of polymerisation (DP) of two were hydrolysed to a further extent than longer UAmeXOS (DP 3-4). On the contrary, ReGH115 was able to release UAme from both polymeric UAmexylan and UAmeXOS. ReGH115 cleaved UAme from both internal and non-reducing end xylosyl residues, with the exception of UAme attached to the non-reducing end of a xylotriose oligosaccharide. Conclusion: In this research, and for the first time, we define the mode-of-action of two α-glucuronidases from two different GH families both from the ascomycete R. emersonii. To date, only four α-glucuronidases classified in GH115 are characterised. ReGH67 showed limited substrate specificity towards only UAmeXOS, cleaving UAme only when attached to the non-reducing end xylosyl residue. ReGH115 was much less substrate specific compared to ReGH67, because UAme was released from both polymeric UAmexylan and UAmeXOS, from both internal and non-reducing end xylosyl residues. The characterisation of the mode-of-action of these two α-glucuronidases helps understand how R. emersonii attacks UAmexylan in plant biomass and the knowledge presented is valuable to improve enzyme cocktails for biorefinery applications.

  biorefinery, GH115, GH67, Rasamsonia emersonii, xylo-oligosaccharides, α-glucuronidase

  NCBI PubMed ID: 27195020
  Publication DOI: 10.1186/s13068-016-0519-9
  Journal NLM ID: 101316935
  Publisher: London: BioMed Central
  Correspondence: Kabel MA
  Institutions: DSM Biotechnology Center, Delft, the Netherlands, Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands
  Methods: HPAEC, RP-HPLC, UPLC-MS/MS, 2-aminobenzoic acid labelling
  
   
  
  Rasamsonia emersonii CBS 393.64 * Aspergillus niger
  CSDB ID 42807 (all data & tools)