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Literature summary for 1.11.1.14 extracted from

  • Zhang, Z.; Wang, J.; Fan, Y.; Liu, L.; Shun, Q.; Shi, W.; Liu, X.; Wang, F.
    The synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid-state fermentation substrate on enzyme-catalyzed oxidative degradation of lignin (2019), J. Chem. Technol. Biotechnol., 94, 1480-1487 .
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten analogous model is applied to fit experimental data of lignin oxidative degradation. The apparent Michaelis constant of purified LiP product (3.02 mg/ml) is lower than that of the crude LiP solution (4.74 mg/ml), and the apparent maximum reaction rate of the purified LiP product (1.15mg/ml/h) is higher than that of the crude LiP solution (0.86 mg/ml/h). The maximum Ytrs (49.8%) is obtained when the beta-glucosidase activity is 0. The activities of LiP, endo-beta-1,4-glucanase and exo-beta-1,4-glucanase are 10.77, 3.360 and 3.427 U/ml (3:1:1), respectively. The components and structure of the substrate is extremely different before and after synergistic action under optimal conditions. Comparison of kinetic parameters between crude enzyme solution and purified product, detailed overview Aspergillus oryzae

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Aspergillus oryzae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 veratryl alcohol + H2O2 Aspergillus oryzae
-
 2 veratryl aldehyde + 2 H2O
-
 ?
2 veratryl alcohol + H2O2 Aspergillus oryzae CGMCC5992
-
 2 veratryl aldehyde + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-
Aspergillus oryzae CGMCC5992
-
-
-

Purification (Commentary)

Purification (Comment) Organism
extracellular native enzyme by ultrafiltration and anion exchange chromatography, followed by ultrafiltration and gel filtration Aspergillus oryzae

Source Tissue

Source Tissue Comment Organism Textmining
additional information solid-state fermentation Aspergillus oryzae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 veratryl alcohol + H2O2
-
 Aspergillus oryzae 2 veratryl aldehyde + 2 H2O
-
 ?
2 veratryl alcohol + H2O2
-
 Aspergillus oryzae CGMCC5992 2 veratryl aldehyde + 2 H2O
-
 ?
additional information the maximal yield of total reducing sugar (Ytrs) by synergistic effect analysis between LiP and three enzyme components of cellulase (endo-beta-1,4-glucanase, exo-beta-1,4-glucanase and beta-glucosidase), oxidation and degradation of lignin, overview Aspergillus oryzae ?
-
-
additional information the maximal yield of total reducing sugar (Ytrs) by synergistic effect analysis between LiP and three enzyme components of cellulase (endo-beta-1,4-glucanase, exo-beta-1,4-glucanase and beta-glucosidase), oxidation and degradation of lignin, overview Aspergillus oryzae CGMCC5992 ?
-
-

Synonyms

Synonyms Comment Organism
LIP
-
 Aspergillus oryzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Aspergillus oryzae

Cofactor

Cofactor Comment Organism Structure
heme
-
 Aspergillus oryzae

General Information

General Information Comment Organism
physiological function synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid-state fermentation substrate on enzyme-catalyzed oxidative degradation of lignin. beta-Glucosidase is the key enzyme that inhibits the oxidative degradation of lignin. The results lay the foundation for screening and optimizing fermentation process conditions of the LiP strain, and improving the efficiency of enzyme-catalyzed oxidative degradation of lignin Aspergillus oryzae