S. Tagger

Hebrew University of Jerusalem

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Jérémy Petit

Université de Lorraine

Criquet Stéven

Institut Méditerranéen de Biodiversité et d'Ecologie Marine et Continentale

Anne‐Marie Farnet

Institut Méditerranéen de Biodiversité et d'Ecologie Marine et Continentale

Jean Le Petit

Institut Méditerranéen de Biodiversité et d'Ecologie Marine et Continentale

G. Gil

Sabin Medicina Diagnostica (Brazil)

Günter Vogt

Heidelberg University

L. Deveze

Aix-Marseille Université

Gilles Iacazio

Centrale Marseille

Claude Périssol

Aix-Marseille Université

Ellen R. Gräber

Agricultural Research Organization

Cooperative Institutions

Centre National de la Recherche Scientifique

Aix-Marseille Université

Institut de Microbiologie de la Méditerranée

Institut Méditerranéen de Biodiversité et d'Ecologie Marine et Continentale

Institut de Recherche pour le Développement

Institut Fresnel

Société du Canal de Provence

Laboratoire d'Informatique, de Modélisation et d'Optimisation des Systèmes

Université de Montpellier

Laboratoire de Chimie

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Preliminary study on relationships among strains forming a bacterial community selected on naphthalene from a marine sediment

Canadian Journal of Microbiology (1990)

S. Tagger Nìcole Truffaut Jérémy Petit

Two bacterial strains were isolated from a bacterial community formed of nine strains, selected from a marine sediment on a seawater medium with naphthalene as sole carbon source. The two strains studied in the present work were the only strains of this community able to grow in pure culture on naphthalene; therefore, they were called "primary" strains. The seven other strains were maintained in the community by using metabolic intermediates of the two primary strains; they were called "auxiliary" strains. Regulation of naphthalene metabolism was studied for the two primary strains. They oxidized naphthalene into catechol, which was degraded only by the meta pathway. For Pseudomonas Lav. 4, naphthalene oxygenase and salicylate hydroxylase were inducible; catechol 2,3-dioxygenase was constitutive. For Moraxella Lav. 7, naphthalene oxygenase was constitutive; salicylate hydroxylase and catechol 2,3-oxygenase were inducible. The Moraxella strain carries two cryptic plasmids, about 63-and 85-kb in molecular size. In the bacterial community culture medium, Moraxella Lav. 7 prevented accumulation of 2-hydroxymuconate semialdehyde formed by Pseudomonas Lav. 4. The auxiliary strains take up formic, acetic, pyruvic, propionic, and succinic acids released by the two primary strains. Key words: marine bacterial community, naphthalene metabolism.

Catechol

Moraxella (Branhamella) catarrhalis

Strain (injury)

Pseudomonas stutzeri

Marine bacteriophage

10.1139/m90-115

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Citations (32)

Phenoloxidases of the white-rot fungus Marasmius quercophilus isolated from an evergreen oak litter (Quercus ilex L.)

Enzyme and Microbial Technology (1998)

S. Tagger Claude Périssol G. Gil Günter Vogt Jérémy Petit

Tannin

10.1016/s0141-0229(98)00062-3

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Citations (54)

Biochemical and Molecular Characterization of a Laccase from Marasmius quercophilus

Applied and Environmental Microbiology (2000)

Boghos Dedeyan Agnieszka Klonowska S. Tagger Thierry Tron Gilles Iacazio

ABSTRACT The basidiomycete Marasmius quercophilus is commonly found during autumn on the decaying litter of the evergreen oak ( Quercus ilex L.), a plant characteristic of Mediterranean forest. This white-rot fungus colonizes the leaf surface with rhizomorphs, causing a total bleaching of the leaf. In synthetic liquid media, this white-rot fungus has strong laccase activity. From a three-step chromatographic procedure, we purified a major isoform to homogeneity. The gene encodes a monomeric glycoprotein of approximately 63 kDa, with a 3.6 isoelectric point, that contains 12% carbohydrate. Spectroscopic analysis of the purified enzyme (UV/visible and electron paramagnetic resonance, atomic absorption) confirmed that it belongs to the “blue copper oxidase” family. With syringaldazine as the substrate, the enzyme's pH optimum was 4.5, the optimal temperature was 75°C, and the K m was 7.1 μM. The structural gene, lac1 , was cloned and sequenced. This gene encodes a 517-amino-acid protein 99% identical to a laccase produced by PM1, an unidentified basidiomycete previously isolated from wastewater from a paper factory in Spain. This similarity may be explained by the ecological distribution of the evergreen oak in Mediterranean forest.

10.1128/aem.66.3.925-929.2000

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Citations (123)

Purification, partial characterization, and reactivity with aromatic compounds of two laccases fromMarasmius quercophilusstrain 17

Canadian Journal of Microbiology (2000)

Anne‐Marie Farnet Criquet Stéven S. Tagger G. Gil Jérémy Petit

Two isozymes of laccase were obtained from an induced liquid culture of Marasmius quercophilus with p-hydroxybenzoic acid as the inducer. Both the constitutive and the induced isozyme have a molecular mass of 60 kDa as determined by polyacrylamide gel electrophoresis. Using isoelectric focusing, we found three isozymes with the constitutive enzyme (pI 4, 4.2, 4.4) and four of the induced form (pI 4.75, 4.85, 4.95, 5.1). We observed certain differences between these two isozymes; the specific activity of the induced isozyme was twice as high, and two optimum pH levels (5 and 6) were observed with the induced isozyme (only one, pH 5, for the constitutive isozyme). However, both of these enzymes have the same thermal stability and the same temperature for their highest activity (80°C). Furthermore, the reactivity of both these enzymes with aromatic compounds was similar. The use of mediators extended the oxidized substrate range of the laccases studied. Various products of degradation were observed, depending on the mediator used. When laccase was used alone, the decrease of the signal corresponding to the aromatic cycle, without any formations of other peaks at different wavelengths, suggested polymerisation of aromatic compounds.Key words: laccase, Marasmius quercophilus, mediator, phenol degradation.

Molecular mass

10.1139/w99-138

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Citations (84)

Purification, partial characterization, and reactivity with aromatic compounds of two laccases from <i>Marasmius quercophilus</i> strain 17

Canadian Journal of Microbiology (2000)

Anne‐Marie Farnet Criquet Stéven S. Tagger G. Gil Jérémy Petit

Strain (injury)

Reactivity

10.1139/cjm-46-3-189

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Citations (29)

Endoglucanase and β-glycosidase activities in an evergreen oak litter: annual variation and regulating factors

Soil Biology and Biochemistry (2002)

Criquet Stéven S. Tagger Günter Vogt Jérémy Petit

Litter

Plant litter

Biotic component

Decomposer

10.1016/s0038-0717(02)00045-7

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Citations (63)

Dégradation des hydrocarbures en présence d'autres substances organiques par des bactéries isolées de l'eau de mer

Canadian Journal of Microbiology (1976)

Jérémy Petit S. Tagger

Three bacterial strains, isolated on gas-oil from seawater, have a variously changed growth on hexadecane with supply of two organic substances. Acetate reduces growth of all tested strains and particularly the hexadecane degradation by Acinetobacter sp. On the contrary, trypticase-phytone promotes the degradation by the three strains.

Hexadecane

10.1139/m76-243

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Citations (4)

Annual variations of phenoloxidase activities in an evergreen oak litter: influence of certain biotic and abiotic factors

Soil Biology and Biochemistry (2000)

Criquet Stéven Anne‐Marie Farnet S. Tagger Jérémy Petit

Biotic component

Litter

10.1016/s0038-0717(00)00027-4

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Citations (115)

Quelques donnees sur l'ecologie d'une zone marine littorale recevant les rejets d'une raffinerie de petrole

Environmental Pollution (1970) (1977)

Jérémy Petit Martine Herviou Nguyen S. Tagger

10.1016/0013-9327(77)90032-5

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Citations (8)

Dégradation biologique de la litière de chêne vert dans deux forêts de la région provençale (Var, France)

Ecologia mediterranea (1984)

Alain Chabert Jérémy Petit Roger Loisel Robert Matheron S. Tagger

Le but de ce travail a été de caractériser l 'activité biologique dans la litière de Chêne vert en deux stations. Les méthodes utilisées ont mis en évidence des différences dans les activités respiratoires et phosphatase alcalins. Les autres activités enzymatiques (phosphatases acides , uréases et catéchol-oxygénases) sont très élevées et ne permettent pas une distinction entre les stations. Aucune activité nitrogénasique n'a été décelée.

10.3406/ecmed.1984.1055

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Citations (3)