Interference of peptone and tyrosine with the lignin peroxidase assay

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منابع مشابه

Interference of peptone and tyrosine with the lignin peroxidase assay.

The N-unregulated white rot fungus Bjerkandera sp. strain BOS55 was cultured in 1 liter of peptone-yeast extract medium to produce lignin peroxidase (LiP). During the LiP assay, the oxidation of veratryl alcohol to veratraldehyde was inhibited due to tyrosine present in the peptone and the yeast extract.

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15 صفحه اول

On the interaction of lignin peroxidase with lignin

The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Veratryl alcohol (Valc), a secondary metabolite of white rot fungi, acts as a cofactor for the enzyme. The Lip-redox cycle is discussed in terms of Marcus theory of electron transfer. It is proposed that reaction of a nucleophile in the active site channel with the incipient Valc'. is an essential eve...

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Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism.

LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) instead of the tryptophan conserved in other lignin-degrading peroxidases. Pristine LiP showed a lag period in VA (veratryl alcohol) oxidation. However, VA-LiP (LiP after treatment with H2O2 and VA) lacked this lag, and H2O2-LiP (H2O2-treated LiP) was inactive. MS analyses revealed that VA-LiP in...

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Lignin Peroxidase Of

Ligninase is a generic name for a group of isozymes that catalyze the oxidative depolymerization of lignin. Although undoubtedly produced by other lignin-degrading fungi, these isozymes to data have been isolated only from the basidiomycete Phanerochaete chrysosporium Burds. 1,2 These ligninases are extracellular and are produced during secondary metabolism, brought about by nutrient starvation...

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 1997

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.63.8.3301-3303.1997