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Literature summary extracted from

  • Shahid, S.; Tajwar, R.; Akhtar, M.W.
    A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities (2018), Extremophiles, 22, 109-119 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.8 food industry the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass Acidothermus cellulolyticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 expressed in Escherichia coli BL21 Codon Plus (DE3) RIPL cells Acidothermus cellulolyticus
3.2.1.8 gene xyn10B, sequence comparisons, recombinant expression in Escherichia coli strain BL21 CodonPlus (RIPL) Acidothermus cellulolyticus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 Ca2+ about 90% residual activity at 1 mM Acidothermus cellulolyticus
3.2.1.8 EDTA about 78% residual activity at 50 mM Acidothermus cellulolyticus
3.2.1.8 Mn2+ 40% inhibition at 1 mM; about 55% residual activity at 1 mM Acidothermus cellulolyticus
3.2.1.8 additional information no inhibition by 1-10 mM EDTA Acidothermus cellulolyticus
3.2.1.8 Ni2+ about 95% residual activity at 1 mM Acidothermus cellulolyticus
3.2.1.8 SDS 20% inhibition at 0.5%; about 78% residual activity at 0.5% (w/v) Acidothermus cellulolyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
 additional information Km value for Xyn10B with 0.5% beechwood xylan is 2.5 mg/ml Acidothermus cellulolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.8 Mg2+ slight increase of activity at 1 mM Acidothermus cellulolyticus
3.2.1.8 additional information not influenced by Cu2+ Acidothermus cellulolyticus
3.2.1.8 additional information poor effects by 1 mM of Ni2+, Ca2+, Mg2+, Fe3+, and Cu2+ Acidothermus cellulolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.72 Acidothermus cellulolyticus A0LR95 cf. EC 3.2.1.8
-
3.1.1.72 Acidothermus cellulolyticus 11B A0LR95 cf. EC 3.2.1.8
-
3.2.1.8 Acidothermus cellulolyticus A0LR95
-
-
3.2.1.8 Acidothermus cellulolyticus 11B A0LR95
-
-
3.2.1.8 Acidothermus cellulolyticus ATCC 43068 A0LR95
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 recombinant enzyme Xyn10B 10fold from Escherichia coli strain BL21 CodonPlus (RIPL) to homogeneity by adsorption chromatography on amorphous cellulose resin, dialysis, and ultrafiltration Acidothermus cellulolyticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.72 17250
-
 pH 6.0, 70°C Acidothermus cellulolyticus
3.2.1.8 1833
-
 purified recombinant enzyme, pH 6.0, 70°C, substrate beechwood xylan Acidothermus cellulolyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.72 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus 4-nitrophenol + acetate
-
 ?
3.1.1.72 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus 11B 4-nitrophenol + acetate
-
 ?
3.1.1.72 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus ATCC 43068 4-nitrophenol + acetate
-
 ?
3.2.1.8 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus 4-nitrophenol + acetate
-
 ?
3.2.1.8 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus 11B 4-nitrophenol + acetate
-
 ?
3.2.1.8 4-nitrophenyl acetate + H2O
-
 Acidothermus cellulolyticus ATCC 43068 4-nitrophenol + acetate
-
 ?
3.2.1.8 4-nitrophenyl alpha-L-arabinofuranoside + H2O
-
 Acidothermus cellulolyticus 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.8 beechwood xylan + H2O best substrate Acidothermus cellulolyticus xylobiose + xylotriose
-
 ?
3.2.1.8 beechwood xylan + H2O best substrate Acidothermus cellulolyticus xylobiose + xylose + ?
-
 ?
3.2.1.8 birchwood xylan + H2O
-
 Acidothermus cellulolyticus xylobiose + ?
-
 ?
3.2.1.8 birchwood xylan + H2O
-
 Acidothermus cellulolyticus xylobiose + xylotriose + ?
-
 ?
3.2.1.8 insoluble xylan + H2O
-
 Acidothermus cellulolyticus ?
-
 ?
3.2.1.8 additional information no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose Acidothermus cellulolyticus ?
-
 ?
3.2.1.8 additional information the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside Acidothermus cellulolyticus ?
-
 ?
3.2.1.8 additional information no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose Acidothermus cellulolyticus 11B ?
-
 ?
3.2.1.8 additional information the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside Acidothermus cellulolyticus 11B ?
-
 ?
3.2.1.8 additional information no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose Acidothermus cellulolyticus ATCC 43068 ?
-
 ?
3.2.1.8 additional information the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside Acidothermus cellulolyticus ATCC 43068 ?
-
 ?
3.2.1.8 oat spelt xylan + H2O
-
 Acidothermus cellulolyticus xylobiose + xylotriose + ?
-
 ?
3.2.1.8 oat spelt xylan + H2O
-
 Acidothermus cellulolyticus xylobiose + ?
-
 ?
3.2.1.8 xylotetraose + H2O
-
 Acidothermus cellulolyticus 2 xylobiose
-
 ?
3.2.1.8 xylotriose + H2O
-
 Acidothermus cellulolyticus xylobiose + xylose
-
 ?
3.2.1.8 xylotriose + H2O
-
 Acidothermus cellulolyticus 11B xylobiose + xylose
-
 ?
3.2.1.8 xylotriose + H2O
-
 Acidothermus cellulolyticus ATCC 43068 xylobiose + xylose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 ? x * 69000, SDS-PAGE Acidothermus cellulolyticus
3.2.1.8 More secondary structure comparisons, overview Acidothermus cellulolyticus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.72 Acel_0180
-
 Acidothermus cellulolyticus
3.1.1.72 Xyn10B
-
 Acidothermus cellulolyticus
3.2.1.8 Acel_0180
-
 Acidothermus cellulolyticus
3.2.1.8 endo-xylanase
-
 Acidothermus cellulolyticus
3.2.1.8 xylanase 10B
-
 Acidothermus cellulolyticus
3.2.1.8 Xyn10B
-
 Acidothermus cellulolyticus
3.2.1.8 Xyn10B the trifunctional enzyme exhibits endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities Acidothermus cellulolyticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.72 70
-
-
 Acidothermus cellulolyticus
3.2.1.8 70
-
-
 Acidothermus cellulolyticus
3.2.1.8 70
-
 recombinant enzyme Acidothermus cellulolyticus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.8 40 85 activity range, inactive below and above, recombinant enzyme, profile overview Acidothermus cellulolyticus
3.2.1.8 50 80 about 60% activity at 50°C, about 750% activity at 60°C, 100% activity at 70°C, about 90% activity at 80°C, no activity at 90°C Acidothermus cellulolyticus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.72 70
-
 stable up to Acidothermus cellulolyticus
3.1.1.72 80
-
 melting temperature Acidothermus cellulolyticus
3.2.1.8 20 70 purified recombinant enzyme, 30 min, completely stable at 20-50°C, 90% activity is retained at 60°C, and 70% at 70°C, inactivation at 80°C Acidothermus cellulolyticus
3.2.1.8 20 80 the enzyme remains completely stable from 20 to 50°C, while about 90 and 70% of the activity is retained at 60 and 70°C after 30 min. The melting temperature is 80°C Acidothermus cellulolyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.72 6
-
-
 Acidothermus cellulolyticus
3.2.1.8 6
-
-
 Acidothermus cellulolyticus
3.2.1.8 6
-
 recombinant enzyme Acidothermus cellulolyticus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 3.5 8.5 activity range, recombinant enzyme, profile overview Acidothermus cellulolyticus
3.2.1.8 5 8 more than 60% activity between pH 5.0 and 8.0 Acidothermus cellulolyticus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.8 5 8 purified recombinant enzyme, stable at Acidothermus cellulolyticus
3.2.1.8 5 8 the enzyme remains completely stable after 30 min incubation between pH 5.0 and 8.0 Acidothermus cellulolyticus

General Information

EC Number General Information Comment Organism
3.1.1.72 physiological function Xyn10B is a trifunctional enzyme having endoxylanase, arabinofuranosidase and acetyl xylan esterase activities. Xyn10B is highly active on birchwood xylan producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains Acidothermus cellulolyticus
3.2.1.8 evolution enzyme Xyn10B belongs to the glycoside hydrolase family 10, GH10 Acidothermus cellulolyticus