Induction of laccase in fungus, Cyathus stercoreus using some aromatic inducers
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Abstract
To improve the feed quality removal of lignin from plant biomass is essential. To improve the activity of laccase of white rot fungi, aromatic inducers are used. In this study three inducers [Resorcinol (5mM and 10mM), Xylidine and Anisaldehyde] to induce the production of laccase enzyme in the culture of fungus: Cyathus stercoreus. Resorcinol (10mM) was found to be the best inducer among the rest. The enzyme activity was observed highest on the 8th day of induction (226.7U/ml). Protein content was also increased with the age of the culture. 80% ammonium sulphate was suitable for precipitating the laccase enzyme for culture filtrate. The laccase production can be enhanced with inducers and can be further used for the removal of lignin from the plant biomass.
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Keywords
Cyathus stercoreus, Enzyme, Fungus, Lignin
References
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Elisashvili, V., Kachlishvili, E., Khardziani, T., Agathos, S.N. (2010). Effect of aromatic compounds on the production of laccase and manganese peroxidase by white-rot basidiomycetes. J Ind. Microbiol. Biotechnol. 37(10):1091-1096. doi: 10.1007/s10295-010-0757-y. Epub 2010 Jun 9.
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Patel, H., Gupte, A., Gupte, S. (2009). Effect of different culture conditions and inducer on production of laccase by a basidiomycetes fungal isolate Pleurotus ostreatus HP-1. Biores. 4(1):268–284.
Patel, H. and Gupte, A. (2016). Optimization of different culture conditions for enhanced laccase production and its purification from Tricholoma giganteum AGHP. Bioresources and Bioprocessing. 3:11.
Placido, J., Capareda, S.(2015). Ligninolytic enzymes: a biotechnological alternative for bioethanol production. Bioresources and Bioprocessing. 2:23.
Pozdniakova, N.N., Nikiforova, S.V., Makarov, O.E., Turkovskaia, O.V. (2011). Effect of polycyclic aromatic hydrocarbons on laccase production by white rot fungus Pleurotus ostreatus D1. Prikl Biokhim Mikrobiol. 47(5):595-601.
Sharma, K. K., Kapoor, M., Kuhad, R. C. (2005). In vivo enzymatic digestion, in vitro xylanase digestion, metabolic analogues, surfactants and polyethylene glycol ameliorate laccase production from Ganoderma sp. kk-02. Lett. Appl. Microbiol. 41:24–31. doi: 10.1111/j.1472-765X.2005.01721.
Wilson, K. and Walker, J. (2000). Practical Biochemistry: Principles and Techniques. Cambridge University Press.
Bains, J., Capalash, N., Sharma, P. (2003). Laccase from a non-melanogenic, alkalotolerant?-proteobacterium JB isolated from industrial wastewater drained soil. Biotechnol Lett. 25(1):155–1159. doi: 10.1023/A:1024569722413.
Chapple, C., Ladisch, M., Meilan, R. (2007). Loosening lignin’s grip on biofuel production. Nat. Biotechnol. 25: 746–748.
Dashtban, M., Schraft, H., Syed, T.A., Qin, W. (2010). Fungal biodegradation and enzymatic modification of lignin. Int. J Biochem. Mol. Biol. 1(1):36:50.
Elisashvili, V., Kachlishvili, E., Khardziani, T., Agathos, S.N. (2010). Effect of aromatic compounds on the production of laccase and manganese peroxidase by white-rot basidiomycetes. J Ind. Microbiol. Biotechnol. 37(10):1091-1096. doi: 10.1007/s10295-010-0757-y. Epub 2010 Jun 9.
Falade, A.O., Nwodo, U.U., Iweriebor, B.C., Green, E., Mabinya, L.V., Okoh, A.I. (2016). Lignin peroxidase functionalities and prospective applications. Microbio. Open. 6(1):e000394
Kunjadia, P.D., Sanghvi, G.V., Kunjadia, A.P., Mukhopadhyay, Dave, G.S., (2016). Role of ligninolytic enzymes of white rot fungi (Pleurotus spp.) grown with azo dyes. Springplus 5(1):1487.
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). Protein measurements with Folin-phenol reagent. J Biol. Chem. 193:265–275.
Kapoor, M., Beg, Q.K., Bhushan, B., Dadhich, K.S., Hoondal, G.S. (2000). Production and partial purification and characterization of a thermo-alkali stable polygalacturonase from Bacillus sp. MG-cp-2. Process Biochem. 36:467–473. doi:10.1016/S0032-9592(00)00238-7
Mayer, A.M., Staples, R.C. (2002). Laccase: new functions for an old enzyme. Phytochemistry. 60:551–565.
Mazumder, S., Basu, K.S., Mina, M. (2009). Laccase production in solid state and submerged fermentation by Pleurotus ostreatus. Eng. Life Sci. 9: 45-52.
Mendoza, L., Jonstrup, M., Hatti-Kaul, R., Mattiasson, B. (2011). Azo dye decolorization by a laccase/mediator system in a membrane reactor: enzyme and mediator reusability. Enzyme Microb Technol.49:478–84.
Ministry of new and renewable energy, Government of India (2016). MNRE Annual Report 2015-16, Retrieved on 20 November, 2017 from http://biomasspower.gov.in/About-us-3-Biomass%20Energy%20scenario-4.php.
Mulakhudair, A.R., Hanotu, J., Zimmerman, W. (2017). Exploiting ozonolysis-microbe synergy for biomass processing: Application in lignocellulosic biomass pretreatment. Biomass and bioenergy. 105:147-154.
Patel, H., Gupte, A., Gupte, S. (2009). Effect of different culture conditions and inducer on production of laccase by a basidiomycetes fungal isolate Pleurotus ostreatus HP-1. Biores. 4(1):268–284.
Patel, H. and Gupte, A. (2016). Optimization of different culture conditions for enhanced laccase production and its purification from Tricholoma giganteum AGHP. Bioresources and Bioprocessing. 3:11.
Placido, J., Capareda, S.(2015). Ligninolytic enzymes: a biotechnological alternative for bioethanol production. Bioresources and Bioprocessing. 2:23.
Pozdniakova, N.N., Nikiforova, S.V., Makarov, O.E., Turkovskaia, O.V. (2011). Effect of polycyclic aromatic hydrocarbons on laccase production by white rot fungus Pleurotus ostreatus D1. Prikl Biokhim Mikrobiol. 47(5):595-601.
Sharma, K. K., Kapoor, M., Kuhad, R. C. (2005). In vivo enzymatic digestion, in vitro xylanase digestion, metabolic analogues, surfactants and polyethylene glycol ameliorate laccase production from Ganoderma sp. kk-02. Lett. Appl. Microbiol. 41:24–31. doi: 10.1111/j.1472-765X.2005.01721.
Wilson, K. and Walker, J. (2000). Practical Biochemistry: Principles and Techniques. Cambridge University Press.
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How to Cite
Induction of laccase in fungus, Cyathus stercoreus using some aromatic inducers. (2018). Journal of Applied and Natural Science, 10(1), 445-447. https://doi.org/10.31018/jans.v10i1.1648
