42603
Lignin-Peroxidase
powder, slightly beige, >0.1 U/mg
Synonym(e):
LiP, Ligninase, Peroxidase, Lignin
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Alle Fotos(2)
About This Item
Empfohlene Produkte
Form
powder
Spezifische Aktivität
>0.1 U/mg
Farbe
slightly beige
Versandbedingung
wet ice
Lagertemp.
−20°C
Biochem./physiol. Wirkung
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.
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
Einheitendefinition
1 U entspricht der Enzymmenge, die 1 μmol 3,4-Dimethoxy-benzylalkohol pro Minute bei pH 3.0 und 30°C oxidiert
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Zielorgane
Respiratory system
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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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
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
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