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93014

Sigma-Aldrich

Mangan-Peroxidase

greener alternative

powder, light brown, ≥10 U/g

Synonym(e):

Mangan-abhängige Lignin Peroxidase, MnP, Peroxidase, Mangan

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About This Item

CAS-Nummer:
114995-15-2
EC-Nummer:
1.11.1.13 (BRENDA, IUBMB)
MDL-Nummer:
MFCD03792385
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

fungus (white-rot fungus (Phanerochaete chrysosporium))

Form

powder

Spezifische Aktivität

≥10 U/g

Grünere Alternativprodukt-Eigenschaften

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

sustainability

Greener Alternative Product

Farbe

light brown

Grünere Alternativprodukt-Kategorie

Enabling,

Versandbedingung

wet ice

Lagertemp.

−20°C

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Allgemeine Beschreibung

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

Anwendung

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. Wirkung

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 .

Einheitendefinition

1 U entspricht der Enzymmenge, die 1 mmol Mn2+ to Mn3+ pro Minute bei pH 4.5 und 25°C oxidiert

Physikalische Form

nur teilweise löslich in Wasser oder Puffer
Supplied as a lyophilized powder containing ~50% sodium tartrate

Sonstige Hinweise

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

Piktogramme

Health hazard
GHS08

Signalwort

Danger

H-Sätze

H334

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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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