Degradation of 2-chlorophenol and formation of 2-chloro-1,4-benzoquinone by mycelia and cell-free crude culture liquids ofTrametes versicolor in relation to extracellular laccase activity

Author(s):  
Roland Grey ◽  
Christine Höfer ◽  
Dietmar Schlosser
Author(s):  
Johann Hess ◽  
Christian Leitner ◽  
Christiane Galhaup ◽  
Klaus D. Kulbe ◽  
Barbara Hinterstoisser ◽  
...  

2021 ◽  
Vol 43 ◽  
pp. e51805
Author(s):  
Luciana Furlaneto Maia ◽  
Sérgio Luis Mendes Hoyos ◽  
Alex Kiyomassa Watanabe ◽  
Alane Tatiana Pereira Moralez ◽  
Marcia Cristina Furlaneto ◽  
...  

Laccase is an important enzyme in terms of its versatile applicability, but its commercial use is limited by factors such as high production cost, low activity and/or stability under given conditions. The objective of this study was to screen xylophagic bacteria isolated from termites for the production of extracellular and intracellular laccases. Six laccase-positive strains were isolated, namely CA, A3, A5, A6, A7 and A8. They were molecularly identified by sequence analysis of 16S rRNA and classified under the genera Bacillus (A7, A8, CA) and Pseudomonas (A3, A5, A6). Laccase was produced by these bacterial isolates by submerged fermentation and was optimized at 37°C, pH 5.5, 6.2 and 7.0, with agitation and 0.5 mM guaiacol (as carbon source). Laccase activity was determined by measuring the oxidation of guaiacol and ABTS (2,21-azino bis[3-ethylbenzthiazoline-6-sulfonate]). Strain A5 produced extracellular laccase titers ranging from 123 to 168 U ml-1. Guaiacol was identified as a better substrate for the quantification of laccase. In conclusion, bacteria harboring the gut of termites can produce extracellular laccase with activity at medium to moderate acidity.


2019 ◽  
Vol 46 (2) ◽  
pp. 161-167
Author(s):  
E. G. Ponomareva ◽  
M. A. Kupryashina ◽  
E. P. Vetchinkina ◽  
V. E. Nikitina

Author(s):  
Ivana Ortega Rojas ◽  
Adriana Rodríguez Pérez ◽  
Juan Fernando Cárdenas González ◽  
Víctor Manuel Martínez Juárez ◽  
Erika Enriquez Domínguez ◽  
...  

Aims: The objective of this work was to determine the degradation capacity of low-density polyethylene by the bacterium Bacillus subtilis and analyze the production of extracellular laccase activity. Methodology: The experiments was realized in 50 mL of culture medium, added with a fragment of known dry weight (1 cm2 colorless polyethylene bag squares), and were incubated at 28°C, pH 6.5, for 6 months under static conditions, determining the growth of the bacterium by dry weight (68, 75, and 91 mg), the production of extracellular protein (271, 234, and 326.1 mg/mL), and the degradation of the substrate by dry biodegraded (8.57%, 5.88%, and 11.76%). Results: The production of extracellular laccase enzyme was analyzed in presence of polyethylene, finding an enzymatic activity of laccase of 2.06, 1.49, and 2,03 U/mL, while in the control without substrate, no enzymatic activity was observed, which suggests that this enzyme may participate in the degradation of polyethylene. In addition, some characteristics of the extracellular enzymatic activities were analyzed, such as stability at 4oC and 28oC, optimal pH and temperature, the effect of protein and substrate concentration. Conclusion: The extracellular protein production and dry weight of the bacterium are higher in the presence of low-density polyethylene. The laccase activity is very stable at 4oC and 28oC, the most effective pH and temperature, were 4.5 and 28oC, and present an incubation time of 5 minutes, and this data suggest that this enzymatic activitiy may participate in the degradation of low density polyethylene.


2021 ◽  
Vol 22 (19) ◽  
pp. 10676
Author(s):  
Anna Jasińska ◽  
Adrian Soboń ◽  
Sylwia Różalska ◽  
Paulina Średnicka

Bisphenol (BPA) is a key ingredient in the production of epoxy resins and some types of plastics, which can be released into the environment and alter the endocrine systems of wildlife and humans. In this study, the ability of the fungus M. roridumIM 6482 to BPA elimination was investigated. LC-MS/MS analysis showed almost complete removal of BPA from the growth medium within 72 h of culturing. Products of BPA biotransformation were identified, and their estrogenic activity was found to be lower than that of the parent compound. Extracellular laccase activity was identified as the main mechanism of BPA elimination. It was observed that BPA induced oxidative stress in fungal cells manifested as the enhancement in ROS production, membranes permeability and lipids peroxidation. These oxidative stress markers were reduced after BPA biodegradation (72 h of culturing). Intracellular proteome analyses performed using 2-D electrophoresis and MALDI-TOF/TOF technique allowed identifying 69 proteins in a sample obtained from the BPA containing culture. There were mainly structural and regulator proteins but also oxidoreductive and antioxidative agents, such as superoxide dismutase and catalase. The obtained results broaden the knowledge on BPA elimination by microscopic fungi and may contribute to the development of BPA biodegradation methods.


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