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42603

Sigma-Aldrich

Lignin Peroxidase

powder, slightly beige, >0.1 U/mg

Sinónimos:

LiP, Ligninase, Peroxidase, lignin

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

powder

specific activity

>0.1 U/mg

color

slightly beige

shipped in

wet ice

storage temp.

−20°C

Biochem/physiol Actions

Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded.

Epoxide hydrolase is an enantioselective catalyst for the hydrolytic kinetic resolution of expoxides.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

One unit corresponds to the amount of enzyme, which oxidizes 1 μmole 3.4-dimethoxybenzyl alcohol per minute at pH 3.0 and 30 °C

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

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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Nikita A Khlystov et al.
Communications biology, 4(1), 1027-1027 (2021-09-03)
Lignin has significant potential as an abundant and renewable source for commodity chemicals yet remains vastly underutilized. Efforts towards engineering a biochemical route to the valorization of lignin are currently limited by the lack of a suitable heterologous host for
E N Jacobsen
Accounts of chemical research, 33(6), 421-431 (2000-07-13)
The discovery of the metal salen-catalyzed asymmetric ring-opening (ARO) of epoxides is chronicled. A screening approach was adopted for the identification of catalysts for the addition of TMSN(3) to meso-epoxides, and the chiral (salen)CrN(3) complex was identified as optimal. Kinetic
Andrew T Smith et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(38), 16084-16089 (2009-10-07)
The surface oxidation site (Trp-171) in lignin peroxidase (LiP) required for the reaction with veratryl alcohol a high-redox-potential (1.4 V) substrate, was engineered into Coprinus cinereus peroxidase (CiP) by introducing a Trp residue into a heme peroxidase that has similar

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