Four different laccase-producing strains were isolated from arid soils and used for bisphenol A (BPA) degradation. These strains were identified as Chaetomium strumarium G5I, Thielavia arenaria CH9, Thielavia arenaria HJ22 and Thielavia arenaria SM1(III) by internal transcribed spacer 5.8 S rDNA analysis. Residual BPA was evaluated by HPLC analysis during 48 h of incubation. A complete removal of BPA was observed by the whole cell fungal cultures within different times, depending on each strain. C. strumarium G5I was the most efficient degrader, showing 100% of removal within 8 h of incubation. The degradation of BPA was accompanied by the production of laccase and dye decolorizing peroxidase (DyP) under degradation conditions. The presence of aminobenzotriazole (ABT) as an inhibitor of cytochrome P450s monooxygenases (CYP) demonstrated a slight decrease in BPA removal rate, suggesting the effective contribution of CYP in the conversion. The great involvement of laccase in BPA transformation together with cell-associated enzymes, such as CYP, was supported by the identification of hydroxylated metabolites by ultra-high performance liquid chromatography-mass spectroscopy (UHPLC-MS). The metabolic pathway of BPA transformation was proposed based on the detected metabolites. The acute toxicity of BPA and its products was investigated and showed a significant reduction, except for T. arenaria SM1(III) that did not caused reduction of toxicity (IC < 8%), possibly due to the presence of toxic metabolites. The results of the present study point out the potential application of the isolated ascomycetes in pollutant removal processes, especially C. strumarium G5I as an efficient degrader of BPA.
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http://dx.doi.org/10.1016/j.ecoenv.2018.02.077 | DOI Listing |
Appl Microbiol Biotechnol
November 2018
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing, 100081, People's Republic of China.
A new cellulase (TaCel45) of glycoside hydrolase family 45 was identified in the thermophilic fungus Thielavia arenaria XZ7 and was successfully expressed in Pichia pastoris. The specific activities of TaCel45 towards lichenin, sodium carboxymethylcellulose (CMC-Na), and barley β-glucan were 769, 498, and 486 U/mg protein, respectively, which are higher than the values for all other reported GH45 cellulases. TaCel45 had maximum activity at pH 5.
View Article and Find Full Text PDFEcotoxicol Environ Saf
July 2018
Department of Microbiology, University of Granada, Campus Cartuja E-18071, Granada, Spain; Institute of Water Research, University of Granada, Ramón y Cajal 4, E-18071 Granada, Spain.
Four different laccase-producing strains were isolated from arid soils and used for bisphenol A (BPA) degradation. These strains were identified as Chaetomium strumarium G5I, Thielavia arenaria CH9, Thielavia arenaria HJ22 and Thielavia arenaria SM1(III) by internal transcribed spacer 5.8 S rDNA analysis.
View Article and Find Full Text PDFJ Agric Food Chem
December 2014
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences , Beijing 100081, People's Republic of China.
Thermophilic endo-polygalacturonases with high catalytic efficiency are of great interest in the food and feed industries. This study identified an endo-polygalacturonase gene (pg7fn) of glycoside hydrolase family 28 in the thermophilic fungus Thielavia arenaria XZ7. Recombinant PG7fn produced in Pichia pastoris is distinguished from other enzyme counterparts by its high functional temperature (60 °C) and specific activity (34382 ± 351 U/mg toward polygalacturonic acid).
View Article and Find Full Text PDFAppl Microbiol Biotechnol
September 2013
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No.12 Zhongguancun South Street, Beijing, 100081, People's Republic of China.
A novel β-mannanase gene, man5XZ7, was cloned from thermophilic fungus Thielavia arenaria XZ7, and successfully expressed in Pichia pastoris. The gene (1,110 bp) encodes a 369-amino acid polypeptide with a molecular mass of approximately 40.8 kDa.
View Article and Find Full Text PDFJ Biotechnol
November 2011
Laboratory of Biotechnology, Lamberti S.p.A., via Piave 18, 21041 Albizzate (VA), Italy.
Chemical modifications of galactomannans are applied to improve and/or modify their solubility, rheological and functional properties, but have limited specificity and are often difficult to control. Enzymatic reactions, catalyzed under mild process conditions, such as depolymerization, debranching and oxidation, represent a viable and eco-friendly alternative. In this study, we describe oxidation of guar galactomannan primary hydroxyl groups by a fungal laccase using the stable radical TEMPO as mediator.
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