93014
Manganese peroxidase from white-rot fungus (Phanerochaete chrysosporium)
powder, light brown, ≥10 U/g
Synonym(s):
Manganese-dependent lignin peroxidase, MnP, Peroxidase, manganese
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About This Item
CAS Number:
MDL number:
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
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sustainability
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color
light brown
greener alternative category
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 .
Physical form
Supplied as a lyophilized powder containing ~50% sodium tartrate
only partially soluble in water or buffer
Other Notes
One unit corresponds to the amount of enzyme, which oxidizes 1 μmole Mn2+ per minute to Mn3+ at pH 4.5 and 25 °C
This product is supplied as a mixture of isozymes, mol. mass (40-65 kDa).
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Tatsuki Sugiura et al.
FEMS microbiology letters, 331(1), 81-88 (2012-04-18)
We identified a highly expressed protein (BUNA2) by two-dimensional gel electrophoresis from the hyper lignin-degrading fungus Phanerochaete sordida YK-624 under wood-rotting conditions. Partial amino acid sequences of BUNA2 were determined by LC-MS/MS analysis, and BUNA2 gene (bee2) and promoter region
Hiroshi Nishimura et al.
Organic & biomolecular chemistry, 10(31), 6432-6442 (2012-06-29)
New ceriporic acids-alkadienyl and alkenyl itaconic acids having a bis-allyl (3-[(Z,Z)-hexadec-7,10-dienyl]-itaconic acid; ceriporic acid G) and a monoene (3-[(Z)-octadec-9-enyl]-itaconic acid; ceriporic acid H) structure in their side chains-were isolated from the cultures of the selective lignin-degrading fungus Ceriporiopsis subvermispora. The
Guanyu Zheng et al.
Bioresource technology, 126, 397-403 (2012-04-24)
A novel approach was developed using oil-in-water (O/W) microemulsions formed with non-ionic surfactant, cosurfactant (1-pentanol) and linseed oil, at the cosurfactant to surfactant ratio (C/S ratio, w/w) of 1:3 and oil to surfactant ratio (O/S ratio, w/w) of 1:10, to
Yi-ru Chen et al.
Methods in molecular biology (Clifton, N.J.), 908, 251-268 (2012-07-31)
Over the past three decades, the activities of four kinds of enzyme have been purported to furnish the mechanistic foundations for macromolecular lignin depolymerization in decaying plant cell walls. The pertinent fungal enzymes comprise lignin peroxidase (with a relatively high
M A Kupriashina et al.
Prikladnaia biokhimiia i mikrobiologiia, 48(1), 23-26 (2012-05-10)
Homogenous Mn-peroxidase of a 26-fold purity grade was isolated from a culture of Azospirillum brasilense Sp245 cultivated on a medium containing 0.1 mM pyrocatechol. The molecular weight of the enzyme is 43 kD as revealed by electrophoresis in SDS-PAAG. It
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