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Literature summary extracted from

  • He, J.; Yu, B.; Zhang, K.; Ding, X.; Chen, D.
    Expression of endo-1,4-beta-xylanase from Trichoderma reesei in Pichia pastoris and functional characterization of the produced enzyme (2009), BMC Biotechnol., 9, 56.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 gene Xyn2, expression in Pichia pastoris under the control of the methanol inducible alcohol oxidase 1, AOX1, promoter. The recombiannt enzyme is secreted to the culture medium Trichoderma reesei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
 additional information kinetics Trichoderma reesei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 21000
-
 x * 21000, recombinant enzyme, SDS-PAGE Trichoderma reesei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O Trichoderma reesei
-
 ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O Trichoderma reesei RUT C-30
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Trichoderma reesei B2CNY5 gene xyn2
-
3.2.1.8 Trichoderma reesei RUT C-30 B2CNY5 gene xyn2
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 additional information
-
 purified recombinant enzyme, 281.2 U/ml with birchwood xylan, 211.0 U/ml with beechwood xylan, and 261.0 U/ml with oat spelt xylan Trichoderma reesei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O
-
 Trichoderma reesei ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O xylan from birchwood, beechwood, and oat spelt Trichoderma reesei ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O
-
 Trichoderma reesei RUT C-30 ?
-
 ?
3.2.1.8 beta-1,4-xylan + H2O xylan from birchwood, beechwood, and oat spelt Trichoderma reesei RUT C-30 ?
-
 ?
3.2.1.8 additional information no activity with Avicel, carboxymethylcellulose, and gellan gum Trichoderma reesei ?
-
 ?
3.2.1.8 additional information no activity with Avicel, carboxymethylcellulose, and gellan gum Trichoderma reesei RUT C-30 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 ? x * 21000, recombinant enzyme, SDS-PAGE Trichoderma reesei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 60
-
-
 Trichoderma reesei

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 50
-
 purified recombinant enzyme, 30 min, 94% activity remaining Trichoderma reesei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.8 139.6
-
 beta-1,4-xylan pH 5.0, 50°C, beechwood xylan Trichoderma reesei
3.2.1.8 168.7
-
 beta-1,4-xylan pH 5.0, 50°C, oat spelt xylan Trichoderma reesei
3.2.1.8 205.7
-
 beta-1,4-xylan pH 5.0, 50°C, birchwood xylan Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 6
-
-
 Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 3 8
-
 Trichoderma reesei