42603
Lignin Peroxidase
powder, slightly beige, >0.1 U/mg
Synonym(s):
LiP, Ligninase, Peroxidase, lignin
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About This Item
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.
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
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
常规特殊物品
Certificates of Analysis (COA)
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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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