Purification and characterization of a novel laccase from the ascomycete Trichoderma atroviride: Application on bioremediation of phenolic compounds |
| |
| Affiliation: | 1. Laboratoire des Bioprocédés, Centre de Biotechnologie de Sfax BP “1177”, 3018 Sfax, Tunisia;2. Centro de Investigaciones Biológicas (CSIC), Ramiro de Maeztu 9, E-28040 Madrid, Spain;1. Institut Européen des Membranes (IEM), UMR 5635 (CNRS-ENSCM-UM2), Université de Montpellier II, Place Eugène Bataillon, 34095 Montpellier, France;2. CNRS, UMR 5236 (CNRS-CPBS), 1919 Route de Mende, 34293 Montpellier, France;3. Internationales Hochschulinstitut (IHI), Technische Universität Dresden, Markt 23, D-02763 Zittau, Germany;1. Chemical Engineering Research Center, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China;2. State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin 300072, PR China;3. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, PR China;4. Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin University, Tianjin 300072, PR China;1. Microorganism Fermentation Engineering and Technology Research Center of Anhui Province, Anhui Polytechnic University, Central Beijing Road, Wuhu 241000, China;2. School of Biological and Chemical Engineering, Anhui Polytechnic University, Central Beijing Road, Wuhu 241000, China;1. Bioprocess and Biomaterials Laboratory, Department of Microbial Biotechnology, Bharathiar University, Coimbatore 641046, India;2. Bioremediation Laboratory, Department of Microbiology, Periyiar University, Salem 636011, India;3. Department of Extension, Career Guidance and Students Welfare, Bharathiar University, Coimbatore 641046, India |
| |
| Abstract: | The extracellular laccase produced by the ascomycete Trichoderma atroviride was purified and characterized and its ability to transform phenolic compounds was determined. The purified laccase had activity towards typical substrates of laccases including 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS), dimethoxyphenol (2,6-DMP), syringaldazine and hydroquinone. The enzyme was a monomeric protein with an apparent molecular mass of 80 kDa and an isoelectric point of 3.5. The pH optima for the oxidation of ABTS and 2,6-DMP were 3 and 5, respectively, and the optimum temperature was 50 °C with 2,6-DMP. The laccase was stable at slightly acidic pH (4 and 5). It retained 80% of its activity after 4 h incubation at 40 °C. Under standard assay conditions, Km values of the enzyme were 2.5 and 1.6 mM towards ABTS and 2,6-DMP, respectively. This enzyme was able to oxidize aromatic compounds present in industrial and agricultural wastewater, as catechol and o-cresol, although the transformation of chlorinated phenols required the presence of ABTS as mediator. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
