Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.16 extracted from

  • Ravichandran, A.; Rao, R.G.; Gopinath, S.M.; Sridhar, M.
    Augmenting versatile peroxidase production from Lentinus squarrosulus and its role in enhancing ruminant feed (2021), BioResources, 16, 1600-1615 .
No PubMed abstract available

Application

Application Comment Organism
agriculture use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants Lentinus squarrosulus

Protein Variants

Protein Variants Comment Organism
additional information immobilization of Lentinus squarrosulus on inert polyurethane foam (PUF) with optimized medium for production enhances the versatile peroxidase yield multifold. Maximal yield of versatile peroxidase achieved through optimization and immobilization strategies is 116 U/ml Lentinus squarrosulus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Lentinus squarrosulus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ though copper is not directly involved in the activity of versatile peroxidase, copper is an activator for multiple catabolic enzymes such as lytic polysaccharide monooxygenases (LPMO) and glyoxal oxidases that are indirectly involved with versatile peroxidase activity Lentinus squarrosulus
Fe2+ in the heme group Lentinus squarrosulus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2 Lentinus squarrosulus
-
2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2 Lentinus squarrosulus 12292 ITS
-
2 Mn(III) + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Lentinus squarrosulus
-
-
-
Lentinus squarrosulus 12292 ITS
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information strains from solid-state and from submerged fermentations. The fungus produces high levels of versatile peroxidase at a C:N ratio of approximately 100, temperature of 35°C, and initial pH of 7.0. Evaluation and optimization of growth medium and production conditions, detailed overview. Versatile peroxidase production with Cu2+ exhibits the most remarkable effect followed by Zn2+. With all factors appropriate for production of versatile peroxidase, significant enzyme activity is detected in 3 days in the optimized culture medium Lentinus squarrosulus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2
-
Lentinus squarrosulus 2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2
-
Lentinus squarrosulus 12292 ITS 2 Mn(III) + 2 H2O
-
?
additional information Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin Lentinus squarrosulus ?
-
-
additional information Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin Lentinus squarrosulus 12292 ITS ?
-
-
Reactive Black 5 + 2 H+ + H2O2
-
Lentinus squarrosulus oxidized Reactive Black 5 + 2 H2O
-
?
Reactive Black 5 + 2 H+ + H2O2
-
Lentinus squarrosulus 12292 ITS oxidized Reactive Black 5 + 2 H2O
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
assay at Lentinus squarrosulus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
assay at Lentinus squarrosulus

Cofactor

Cofactor Comment Organism Structure
heme
-
Lentinus squarrosulus

General Information

General Information Comment Organism
evolution versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase. This enzyme possesses the catalytic features of oxidation of aromatic compounds through long-range electron transfer (LRET) and Mn (II) to Mn (III), analogous to the latter peroxidase Lentinus squarrosulus
metabolism ligninases, including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase, are crucial components of the ligninolytic machinery. The white-rot fungi engage collective action of these enzymes in mineralization of the complex macromolecule Lentinus squarrosulus
additional information versatile peroxidase is endowed with polyvalent catalytic sites that render this protein with high redox potential Lentinus squarrosulus
physiological function Lentinus squarrosulus is a saprophytic white-rot producing novel versatile peroxidase that is capable of selectively degrading lignin of the crop residues. Treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification Lentinus squarrosulus