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93014

Sigma-Aldrich

Manganese peroxidase from white-rot fungus (Phanerochaete chrysosporium)

greener alternative

powder, light brown, ≥10 U/g

Sinónimos:

Manganese-dependent lignin peroxidase, MnP, Peroxidase, manganese

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About This Item

Número de CAS:
114995-15-2
Comisión internacional de enzimas:
1.11.1.13 (BRENDA, IUBMB)
MDL number:
MFCD03792385
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (white-rot fungus (Phanerochaete chrysosporium))

form

powder

specific activity

≥10 U/g

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

color

light brown

greener alternative category

Enabling,

shipped in

wet ice

storage temp.

−20°C

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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell and cellulosic ethanol research. For more information see the article in biofiles and Enzymes for Alternative Energy Research

Application

Manganese peroxidase from white-rot fungus (Phanerochaete chrysosporium) is from the peroxidase family and is used to oxidize manganese. It may be used to study wound healing.

Biochem/physiol Actions

Manganese peroxidase catalyzes the oxidation of Mn2+ to Mn3+. Mn3+ is then in complex with oxalate, which is able to oxidize lignin. Manganese peroxidase from Phanerochaete chrysosporium binds 2 calcium ions per subunit. It binds 1 heme B (iron-protoporphyrin IX) group per subunit .

Unit Definition

One unit corresponds to the amount of enzyme, which oxidizes 1 μmole Mn2+ per minute to Mn3+ at pH 4.5 and 25 °C

Physical form

Supplied as a lyophilized powder containing ~50% sodium tartrate
only partially soluble in water or buffer

Other Notes

This product is supplied as a mixture of isozymes, mol. mass (40-65 kDa).

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Almasul Alfi et al.
Journal of bioscience and bioengineering, 128(3), 290-295 (2019-04-08)
Manganese peroxidase (MnP) is a fungal heme-containing enzyme which oxidizes Mn2+ to Mn3+, a diffusible and strong non-specific oxidant capable of attacking bulky phenolic substrates. Therefore, MnP is indispensable in the polymer and paper industries. Previous attempts of MnP expression
Pratibha Yadav et al.
Indian journal of biochemistry & biophysics, 49(1), 42-48 (2012-03-23)
Mn-peroxidase (MnP), a biotechnologically important enzyme was purified for the first time from a plant source Musa paradisiaca (banana) stem, which is an agro-waste easily available after harvest of banana fruits. MnP was earlier purified only from the fungal sources.
Haluk Ertan et al.
Biochimie, 94(5), 1221-1231 (2012-05-16)
Isothermal titration calorimetry (ITC) was developed for measuring lignin peroxidase (LiP) and manganese peroxidase (MnP) activities of versatile peroxidase (VP) from Bjerkandera adusta. Developing an ITC approach provided an alternative to colorimetric methods that enabled reaction kinetics to be accurately
Ya-Chen Dong et al.
Bioprocess and biosystems engineering, 35(5), 751-760 (2011-11-26)
The lignin-modifying enzymes (LMEs) play an important role in decomposition of agricultural residues, which contain a certain amount of lignin. In this study, the production of LMEs by three co-cultivated combinations of Phlebia radiata, Dichomitus squalens and Ceriporiopsis subvermispora and
Elsa Contreras et al.
Biotechnology progress, 28(1), 114-120 (2011-10-18)
White-rot fungi (WRF) are capable of degrading complex organic compounds such as lignin, and the enzymes that enable these processes can be used for the detoxification of recalcitrant organopollutants. The aim of this study is to evaluate a system based
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