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Wednesday, May 20, 2020 | History

2 edition of Nutritional regulation of lignin degradation by Phanerochaete chrysosporium found in the catalog.

Nutritional regulation of lignin degradation by Phanerochaete chrysosporium

T. W. Jeffries

Nutritional regulation of lignin degradation by Phanerochaete chrysosporium

by T. W. Jeffries

  • 26 Want to read
  • 18 Currently reading

Published by U.S.G.P.O. in [Washington, D.C.] .
Written in English

    Subjects:
  • Lignin -- Biodegradation.,
  • Wood -- Deterioration.,
  • Wood -- Microbiology.,
  • Phanerochaete chrysosporium.

  • Edition Notes

    Other titlesApplied and environmental microbiology.
    StatementThomas W. Jeffries, Suki Choi, and T. Kent Kirk.
    ContributionsChoi, Suki., Kirk, T. Kent.
    The Physical Object
    Paginationp. 290-296 :
    Number of Pages296
    ID Numbers
    Open LibraryOL22400206M

      The influence of Zn2+ ( × 10−3 – × 10−3 μM) and Cu2+ (4 × 10−4 – × 10−4 μM) in the basal medium on mycelial growth (dry weight), activities of lignin peroxidase (Lip), manganese peroxidase (Mnp), solubilization, and mineralization (14CO2 evolution) of lignin during a period of 3 weeks was studied in Phanerochaete chrysosporium strain MTCCCited by: Nutritional Regulation of Synthetic Lignin (DHP) Degradation by the Selective White-rot Fungus Phlebia (Merulius) tremellosa: Effects of glucose and other cosubstrates.

    Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP).Cited by: The effects of added l-amino acids and on lignin peroxidase activity in ligninolytic cultures of Phanerochaete chrysosporium were investigated. Among 11 arnino acids tested, including phenylalanine, glutamate, glutamine, histidine, alanine, iso-leucine, ornithine, glycine, aspartate, proline, and arginine, phenylalanine was the most effective in suppression of lignin peroxidase by: 8.

    The white-rot fungus Phanerochaete chrysosporium is ca- pable of degrading lignin [l]. The key enzyme of the system is lignin peroxidase (ligninase) [2, This enzyme is a glycopro- tein and has been characterized as a peroxidase [ It catalyses degradation of lignin and low-molecular-mass ligninCited by: “Production of ligninases and degradation of lignin in agitated submerged cultures of Phanerochaete chrysosporium,” Appl. Environ. Microbiol. 50, Kay-Shoemake, J. L., and Watwood, M. E. (). “Limitations of the lignin peroxidase system of the white rot fungus Phanerochaete chrysosporium,” Appl. Microbiol.


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Nutritional regulation of lignin degradation by Phanerochaete chrysosporium by T. W. Jeffries Download PDF EPUB FB2

The balance of trace metals, Mg2+, and Ca2+ was important for lignin degradation. Previous studies have shown that a lignin-degrading system appears in cultures of the white rot fungus Phanerochaete chrysosporium in response to nitrogen starvation, apparently as Cited by: Previous studies have shown that a lignin-degrading system appears in cultures of the white rot fungus Phanerochaete chrysosporium in response to nitrogen starvation, apparently as part of secondary by: Nutritional Regulation of Lignin Degradation by Phanerochaete Chrysosporium.

The amount of lignin degraded depended on the amount of carbohydrate provided, which determined the amount of. Get this from a library.

Nutritional regulation of lignin degradation by Phanerochaete chrysosporium. [Thomas W Jeffries; Suki Choi; T Kent Kirk; Forest Products Laboratory (U.S.)].

Lignin Degradation by Phanerochaete chrysosporium. The study of lignin biodegradation entered the realm of biochemistry in with the first reports of a lignin-degrading enzyme, termed ligninase or lignin peroxidase. The powerful peroxidase was discovered in the basidiomycete Phanerochaete chrysospor-ium, the most studied ligninolytic orga-nism.

When glucose or cellular energy resources were depleted, lignin degradation ceased. The ability of P. chrysosporium to degrade the various lignins in a similar manner and at very low biomass concentrations indicates that the enzymes responsible for lignin degradation are by: microbes [9].

In a previous study, lignin in a tobacco stalk was degraded up to % by Phanerochaete chrysosporium in a period of 15 days. The main enzyme responsible for degradation was found to be laccase [16]. Previous studies assessed that ligninolytic enzymes like laccases and peroxidases cause lignin degradationCited by: 2.

responsible for the oxilative degradation of lignin by the white-rot fungus. Phanerochaete chrysosporium. We examined the hypothesis that activated oxygen species are involved, and we also sought the agent in ligninolytic cultures responsible for a specific oxidative degradative reaction in substructure model compounds.

enzymology-Biomass, part b, lignin, pectin, and chitin. San Diego, CA: Academic Press, Inc.: Vol.[23] Lignin Peroxidase of Phanerochaete chrysosporium By MING TIEN and T.

KENT KIRK Introduction Ligninase is a generic name for a group of isozymes that catalyze the oxidative depolymerization of lignin.

Biodegradation of Orange II, Tropaeolin O, Congo Red, and Azure B in cultures of the white rot fungus, Phanerochaete chrysosporium, was demonstrated by decolarization of the culture medium, the extent of which was determined by monitoring the decrease in absorbance at or near the wavelength maximum for each by: REGULATION OF LIGNIN DEGRADATION poor growth.

Figure 5 shows the effects of 20 and ,uM sulfur in the presence of excess carbohydrate and high or low nitrogen levels. Although all cultures degraded lignin to some extent beginning onday4 or 5 (the usual time foronsetofliginolytic activityundernitrogen- limitedconditions),thesulfur-limited, nitrogen- rich cultures became ligninolytic Cited by: Jeffries TW, Choi S, Kirk TK () Nutritional regulation of lignin degradation by Phanerochaete chrysosporium.

Appl Environ Microbiol – PubMed Google Scholar Johansson T, Welinder KG, Olof Nyman P () Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes by: Printed in Great Britain /97 $ CHLOROPHENOL DEGRADATION BY PHANEROCHAETE CHRYSOSPORIUM R.

Rubio P6rez, G. Gonzfilez Benito* & M. Pefia Miranda Dpto. de Ingenieria Quimica, Facultad de Ciencias, Universidad de Valladolid, Valladolid, Spain (Received 3 December ; revised version received 20 January ; accepted 31 Cited by: Two families of peroxidases—lignin peroxidase (LiP) and manganese-dependent lignin peroxidase (MnP)—are formed by the lignin-degrading white rot basidiomycete Phanerochaete chrysosporium and other white rot fungi.

Isoenzymes of these enzyme families carry out reactions important to the biodegradation of by: Laws and Regulations - (DD) Degradation of lignin by Phanerochaete chrysosporium.

Author(s): Schoemaker, Phanerochaete chrysosporium, phytopathology, Stereales Broader term(s): eukaryotes eukaryotes Subject Category: Organism Names see more details, Polyporales Cited by: A supplement of KH 2 PO 4, MgSO 4, CaCl 2, trace elements, and thiamine accelerated the initial rate of aspen wood decay by Phanerochaete chrysosporium but did not increase the extent of lignin degradation.

Asparagine, casein hydrolysate, and urea supplements (1% added N) strongly inhibited lignin degradation and weight by: Jeffries TW, Choi S, Kirk TK () Nutritional regulation of lignin degradation inPhanerochaete chrysosporium.

Appl Environ Microbiol – Google Scholar Keyser P, Kirk TK, Zeikus JG () Ligninolytic enzyme system of Phanerochaete chrysosporium: synthesized in absence of lignin in response to nitrogen by: B H U T T E R W O R T H E I N E M A N N Physiological regulation of glyoxal oxidase from Phanerochaete chrysosporium by peroxidase systems Bernard Kurek* and Philip J.

Kerstent *Laboraaoorye de Chimie Biologique, Centre de Biotechnologies Agro-Industrielles, Institut National de la Recherche Agronomique, Thiverval-Grignon, France FForest Products Laboratory, Forest Service, Cited by: The results indicate that glucose oxidase activity is the primary source of H2O2 in ligninolytic cultures of P.

chrysosporium and that nutritional parameters which affect lignin degradation have a Author: Ian D Reid. Phanerochaete chrysosporium completely degrades lignocellulose. The most recalcitrant component, lignin, is oxidized by the radical products of lignin and manganese peroxidases, whereas cellulose and hemicellulose are hydrolysed.

Both peroxidases and cellulases exist as complex families at both the DNA and protein by:. The compositions and percentages of lignin and hemicellulose vary from one plant species to another so it is difficult to Nutritional regulation of lignin degradation by Phanerochaete chrysosporium.

Appl. Environ. () Water soluble products from the degradation of aspen lignin by Phanerochaete chrysosporium Can. J. Bot. Cited by:   Two important lignin-degrading fungi with existing or potential applications in the production of food, feed and/or fiber products from wood are Lentinus edodes (Berk.; Sing.=Lentinula edodes [Pegler]) and Phanerochaete chrysosporium (Burds).

This study discusses their relative ability to degrade lignin and the factors controlling their ligninolytic activity (synthetic 14C-lignin→14CO2).Cited by: Phanerochaete chrysosporium spores were immobilized both in agarose and agar gel beads, and used for the production of lignin peroxidase in repeated batch cultures on carbon-limited medium both with g l −1 glucose and without glucose.

Veratryl alcohol was used as an activator of enzyme production. The biocatalyst was more stable in agarose gel with the maximum activity of U l −1 Cited by: