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1.
Enzyme Microb Technol ; 49(6-7): 517-25, 2011 Dec 10.
Article in English | MEDLINE | ID: mdl-22142726

ABSTRACT

Due to their low substrate specificity, fungal laccases have a great potential in industrial applications, including the bioremediation of colored wastewaters from textile industry. However, the presence of halides in these effluents (up to 1M NaCl) which inhibit laccases is a drawback for bioremediation processes. In order to develop an efficient enzymatic remediation process for textile dye effluent, the possibility to reduce this halide inhibition is conditioned by a better understanding of the phenomenon. The present study gives a detailed account of the kinetics of chloride inhibition of both ABTS (a model substrate) and ABu62 (an anthraquinonic acid dye) oxidations catalyzed by Trametes versicolor laccase (LacIIIb). Chloride inhibition can be described by a mixed model for ABTS and a non-competitive model for ABu62 and both inhibitions are linear suggesting a single inhibitory site for chloride. Experiments were also conducted in presence of both substrates. An apparent activation of laccase was observed in the presence of ABu62 leading to an enhancement of the oxidation rate of ABTS. The extent of activation increased in the presence of chloride anions. Finally, for the first time to our knowledge, we evidenced that inhibition of ABTS oxidation by chloride can be reduced in the presence of ABu62.


Subject(s)
Anthraquinones/metabolism , Chlorides/pharmacology , Laccase/antagonists & inhibitors , Benzothiazoles/metabolism , Biodegradation, Environmental/drug effects , Coloring Agents/metabolism , Fungal Proteins/antagonists & inhibitors , Fungal Proteins/metabolism , Kinetics , Laccase/metabolism , Oxidation-Reduction , Substrate Specificity , Sulfonic Acids/metabolism , Textile Industry , Trametes/enzymology
2.
Cell Mol Life Sci ; 67(3): 369-85, 2010 Feb.
Article in English | MEDLINE | ID: mdl-19844659

ABSTRACT

Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.


Subject(s)
Laccase/chemistry , Amino Acid Sequence , Catalytic Domain , Copper/chemistry , Copper/metabolism , Fungi/enzymology , Laccase/genetics , Laccase/metabolism , Molecular Sequence Data , Oxidation-Reduction , Sequence Alignment , Sequence Homology, Amino Acid , Structure-Activity Relationship
3.
Biotechnol Appl Biochem ; 54(2): 65-84, 2009 Jul 14.
Article in English | MEDLINE | ID: mdl-19594442

ABSTRACT

Inter-cell communication aided by released chemical signals when cell density reaches a critical concentration has been investigated for over 30 years as quorum sensing. Originally discovered in Gram-negative bacteria, quorum-sensing systems have also been studied extensively in Gram-positive bacteria and dimorphic fungi. Microbial communities communicating via quorum sensing employ various chemical signals to supervise their surrounding environment, alter genetic expression and gain advantage over their competitors. These signals vary from acylhomoserine lactones to small modified or unmodified peptides to complex gamma-butyrolactone molecules. The scope of this review is to give an insight into some of the quorum-sensing systems now known and to explore their role in microbial physiology and development of pathogenesis. Particular attention will be dedicated to the signalling molecules involved in quorum-sensing-mediated processes and the potential shown by some of their natural and synthetic analogues in the treatment of infections triggered by quorum sensing.


Subject(s)
Gram-Negative Bacteria/physiology , Gram-Positive Bacteria/physiology , Models, Biological , Quorum Sensing/physiology , Anti-Infective Agents , Gram-Negative Bacteria/pathogenicity , Gram-Positive Bacteria/pathogenicity , Homoserine/analogs & derivatives , Homoserine/physiology , Lactones
4.
Environ Sci Technol ; 42(2): 584-9, 2008 Jan 15.
Article in English | MEDLINE | ID: mdl-18284166

ABSTRACT

In view of compliance with increasingly stringent environmental legislation imposed by regional, national, and supranational (e.g., European Union) authorities, innovative environmental technologies for the treatment of dye-contaminated effluents are necessary in the color industry. In this study, effluents of an industrial dye producer were subjected to distinct treatment trains following an initial qualitative characterization. The effectiveness of ozonation and a treatment using white rot fungi (WRF) and their enzymes were compared with respect to parameters such as residual color, toxicity on human cells, and genotoxicity. A combined ozonation/WRF process was also investigated. The effluent exhibited significant toxicity that was reduced by only 10% through ozonation, whereas the fungal treatment achieved a 35% reduction. A combined treatment (ozone/WRF) caused an abatement of the toxicity by more than 70%. In addition, the initial genotoxicity of the effluent was still present after the ozone treatment, while it was completely removed through the fungal treatment.


Subject(s)
Coloring Agents , Mutagens , Ozone/chemistry , Polyporaceae/metabolism , Water Pollutants, Chemical , Animals , Caco-2 Cells , Coloring Agents/chemistry , Coloring Agents/metabolism , Coloring Agents/toxicity , Humans , Laccase/metabolism , Liver/metabolism , Mutagens/chemistry , Mutagens/metabolism , Mutagens/toxicity , Oxidants/chemistry , Rats , Waste Disposal, Fluid/methods , Water Pollutants, Chemical/chemistry , Water Pollutants, Chemical/metabolism , Water Pollutants, Chemical/toxicity , Water Purification/methods
5.
Chemosphere ; 70(6): 1097-107, 2008 Jan.
Article in English | MEDLINE | ID: mdl-17825354

ABSTRACT

Only few data exist on the metabolites produced during the biotransformation of anthraquinonic dyes by white rot fungi (WRF). During the biotransformation of an anthraquinonic dye Acid Blue 62 (ABu62) using Pycnoporus sanguineus MUCL 41582 strain, it was previously demonstrated that the blue colour of the medium turned to red before complete dye decolourisation. To better understand the phenomenon, this study carried out ABu62 biotransformation with five different WRF strains (Coriolopsis polyzona MUCL 38443, Perenniporia ochroleuca MUCL 41114, Perenniporia tephropora MUCL 41562, P. sanguineus MUCL 38531 and Trametes versicolor MUCL 38412) and compared with P. sanguineus MUCL 41582 previously described. A multi-methodological approach (using capillary electrophoresis, mass spectrometry, HPLC, UV, NMR and IR spectroscopies) was developed to characterise the metabolites involved and monitor their apparition. Seven metabolites were commonly found with all strains, suggesting a common metabolic pathway for ABu62 biotransformation. During the first days, dimer and oligomers of the initial ABu62 molecule were observed: the main one absorbed in the 500nm region, explaining the red colour appearance of the medium. This main metabolite was made up of two molecules of ABu62 linked by an azo bond, minus a cyclohexyl moiety. After a longer incubation time, breakdown products were observed. Based on these products characterizations, a bioconversion pathway was proposed.


Subject(s)
Coloring Agents/metabolism , Fungi/metabolism , Biodegradation, Environmental , Chromatography, High Pressure Liquid , Coloring Agents/chemistry , Electrophoresis, Capillary , Magnetic Resonance Spectroscopy , Molecular Structure , Spectrometry, Mass, Electrospray Ionization
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