Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A |
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| Affiliation: | 1. Department of Biochemistry, Shivaji University, Kolhapur 416004, India;2. Department of Biomedical Engineering and Environmental Sciences, National Tsing Hua University, Hsinchu 30013, Taiwan;1. Department of Biotechnology, Dr. N.G.P. Arts and Science College, Coimbatore 641048, Tamil Nadu, India;2. Department of Biotechnology, School of Life Sciences, Karpagam University, Eachanari, Coimbatore 641021, Tamil Nadu, India;3. Department of Chemistry, Government Arts College, Udumalpet, 642 126 Tiruppur, Tamilnadu, India;1. Institute of Chemistry, Department of Biochemistry and Chemical Technology, Sao Paulo State University, 14800-060 Araraquara, SP, Brazil;2. Faculty of Pharmaceutical Sciences, Department of Food and Nutrition, Sao Paulo State University, 14801-902 Araraquara, SP, Brazil;3. Departamento de Biotecnologia, Escola de Engenharia de Lorena, Universidade de São Paulo, 12602-810 Lorena, SP, Brazil;1. School of Chemistry and Chemical Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, 212013, Jiangsu Province, China;2. School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, 212013, Jiangsu Province, China;1. Anhui Province Key Laboratory of Farmland Ecological Conservation and Pollution Prevention, School of Resources and Environment, Anhui Agricultural University, Hefei 230036, China;2. Barani Agricultural Research Institute, Chakwal, Pakistan;3. Institute for Sustainable Agriculture, Spanish National Research Council, Cordoba 14001, Spain |
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| Abstract: | The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40 °C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30 V. The laccase was stable up to 40 °C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5 h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS. |
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