Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/98232
Type: Artigo de periódico
Title: Ligninases From Chrysonilia Sitophila (tfb-27441 Strain)
Author: Duran N.
Ferrer I.
Rodriguez J.
Abstract: Ligninase found in the extracellular medium of cultures of Chrysonilia sitophila was purifieded by ion exchange chromatography. Sodium dodecylsulfate/polyacrylamide gel electrophoresis allowed the determination of 68,000, 48,300, and 48,000 daltons for the molecular weights of ligninase I, II, and III, respectively. The absorption spectrum of the enzymes indicated the presence of a heme prosthetic group. The absorption maximum of the native enzyme II at 400 nm decreased in the presence of one equivalent of hydrogen peroxide. With an additional equivalent of phenol the maximum at 400 nm shifted to 417 nm. This spectrum is similar to horseradish peroxidase compound II. The pyridine hemochromogen absorption spectrum and iron content indicated that ligninases I, II, and III contained a Fe/heme ratio values of 0.8, 1.3, and 1.2 by a molecule of protein, respectively. These enzymes oxidize lignin efficiently, followed by the fluorescence technique and by the photon emission method. © 1987 Humana Press Inc.
Editor: Humana Press
Rights: fechado
Identifier DOI: 10.1007/BF02798364
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-51249177662&partnerID=40&md5=6a2f61ef67673885ee5c07bfe47abf2c
Date Issue: 1987
Appears in Collections:Unicamp - Artigos e Outros Documentos

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