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Literature summary extracted from

  • Boyce, A.; Walsh, G.
    Purification and characterisation of a thermostable beta-xylosidase from Aspergillus niger van Tieghem of potential application in lignocellulosic bioethanol production (2018), Appl. Biochem. Biotechnol., 186, 712-730 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.37 biofuel production the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production Aspergillus niger
3.2.1.37 industry the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.37 arabinose full activity is observed in the presence of up to 50 mM arabinose. Activity is reduced to 88%, 80% and 70% of maximum activity at 100 mM, 150 mM and 200 mM arabinose, respectively Aspergillus niger
3.2.1.37 D-xylose end-product inhibition Aspergillus niger
3.2.1.37 additional information upon inclusion of glucose (10-200 mM) in the beta-xylosidase assay reaction mixture, the purified enzyme exhibits full activity relative to the control reaction without added glucose Aspergillus niger
3.2.1.37 SDS 10 mM, 45% loss of activity Aspergillus niger
3.2.1.37 ZnSO4 10 mM, 50% loss of activity Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.37 0.7526
-
 4-nitrophenyl beta-D-xylopyranoside 70°C, pH 5 Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.37 120000
-
 SDS-PAGE Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.37 Aspergillus niger
-
-
-
3.2.1.37 Aspergillus niger DSM 22593
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.37 glycoprotein treatment with PNGase F results in a decrease in molecular weight to approximately 85000 Da confirming that the purified enzyme is glycosylated Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.37
-
 Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.37 4-nitrophenyl alpha-L-arabinofuranoside + H2O activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside Aspergillus niger 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.37 4-nitrophenyl alpha-L-arabinofuranoside + H2O activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside Aspergillus niger DSM 22593 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.37 4-nitrophenyl beta-D-glucopyranoside + H2O activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside Aspergillus niger 4-nitrophenol + beta-D-glucopyranose
-
 ?
3.2.1.37 4-nitrophenyl beta-D-glucopyranoside + H2O activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside Aspergillus niger DSM 22593 4-nitrophenol + beta-D-glucopyranose
-
 ?
3.2.1.37 4-nitrophenyl beta-D-xylopyranoside + H2O
-
 Aspergillus niger 4-nitrophenol + beta-D-xylopyranose
-
 ?
3.2.1.37 4-nitrophenyl beta-D-xylopyranoside + H2O
-
 Aspergillus niger DSM 22593 4-nitrophenol + beta-D-xylopyranose
-
 ?
3.2.1.37 beechwood xylan + H2O the purified enzyme acts synergistically with Aspergillus niger endo-1,4-beta-xylanase in the hydrolysis of beechwood xylan Aspergillus niger ?
-
 ?
3.2.1.37 beechwood xylan + H2O the purified enzyme acts synergistically with Aspergillus niger endo-1,4-beta-xylanase in the hydrolysis of beechwood xylan Aspergillus niger DSM 22593 ?
-
 ?
3.2.1.37 additional information during hydrolysis of pretreated straw lignocellulose at 70 °C using a commercial lignocellulosic enzyme cocktail, inclusion of the purified enzyme results in a 19fold increase in the amount of xylose produced after 6 h. No activity is detected on 4-nitrophenyl beta-D-cellobioside Aspergillus niger ?
-
 ?
3.2.1.37 additional information during hydrolysis of pretreated straw lignocellulose at 70 °C using a commercial lignocellulosic enzyme cocktail, inclusion of the purified enzyme results in a 19fold increase in the amount of xylose produced after 6 h. No activity is detected on 4-nitrophenyl beta-D-cellobioside Aspergillus niger DSM 22593 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.37 ? x * 120000, SDS-PAGE Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.37 70 75
-
 Aspergillus niger

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.37 60 77 over 50% of maximum activity is observed from 60°C to 77°C Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.37 60
-
 24 h, enzyme retains full activity. 72 h, 9% loss of activity Aspergillus niger
3.2.1.37 65
-
 24 h, enzyme retains full activity. 72 h, 13% loss of activity Aspergillus niger
3.2.1.37 70
-
 18 h, 48% loss of activity Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.37 4.5
-
-
 Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.37 3.4 5.5 over 69% of maximum activity is observed in the pH range 3.4 to 5.5 Aspergillus niger

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.37 7.458
-
 D-xylose 70°C, pH 5 Aspergillus niger