Hostname: page-component-84b7d79bbc-5lx2p Total loading time: 0 Render date: 2024-07-29T04:21:07.944Z Has data issue: false hasContentIssue false
  • English
  • Français

Isolation and characterization of a novel laccase from an Antarctic thermophilic Geobacillus

Published online by Cambridge University Press:  30 May 2022

Joaquín Atalah Open the ORCID record for Joaquín Atalah [Opens in a new window]  and
Jenny M. Blamey
Joaquín Atalah*
Affiliation:
Fundación Biociencia, José Domingo Cañas 2280, Ñuñoa, Santiago, Chile Facultad de Ciencias Químicas, Universidad de Chile, Santos Dumont 964, Independencia, Santiago, Chile
Jenny M. Blamey
Affiliation:
Fundación Biociencia, José Domingo Cañas 2280, Ñuñoa, Santiago, Chile
*
jatalah@bioscience.cl
Get access Rights & Permissions [Opens in a new window]

Abstract

Laccases are enzymes from the multi-copper oxidase family that have gathered a lot of attention due to their wide range of substrates, their interspecies variability and their still elusive mechanism of action. The presence of four copper atoms in their active site makes them an interesting model for the study of the relationship between the structure and function of proteins. It is possible to find them in fungi, plants and prokaryotes. Bacterial laccases display many advantages over fungal laccases in terms of their application. They have, in general, a greater thermal stability and a different pH profile, which contributes to widening their field of possible application. In the present work, a novel laccase from an Antarctic microorganism, Geobacillus sp. ID17, is purified and characterized. This is the first Antarctic bacterial laccase to be functionally described. It was found to be active at neutral pH and to have greater activity at 55°C. Its catalytic constants are in the order of other bacterial laccases. Screening for different potential substrates was also performed, showing that this novel laccase is more selective than commercial laccases. This enzyme could find potential application in the generation of gallic acid polymers or in organic synthesis in contexts where meticulous substrate discrimination is needed.

Keywords

biotechnologyenzymesGeobacilluslaccasethermophiles
Type
Biological Sciences
Information
Antarctic Science , Volume 34 , Issue 4 , August 2022 , pp. 289 - 297
Check for updates
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of Antarctic Science Ltd

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Atalah, J., Cáceres-Moreno, P., Espina, G. & Blamey, J.M. 2019. Thermophiles and the applications of their enzymes as new biocatalysts. Bioresource Technology, 280, 10.1016/J.BIORTECH.2019.02.008.CrossRefGoogle ScholarPubMed
Basheer, S., Rashid, N., Ashraf, R., Akram, M.S., Siddiqui, M.A., Imanaka, T. & Akhtar, M. 2017. Identification of a novel copper-activated and halide-tolerant laccase in Geobacillus thermopakistaniensis. Extremophiles, 21, 10.1007/s00792-017-0925-3.CrossRefGoogle ScholarPubMed
Berka, R.M., Schneider, P., Golightly, E.J., Brown, S.H., Madden, M., Brown, K.M., et al. 1997. Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Applied and Environmental Microbiology, 63, 3151–3157.CrossRefGoogle ScholarPubMed
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.CrossRefGoogle ScholarPubMed
Claus, H. 2003. Laccases and their occurrence in prokaryotes. Archives of Microbiology, 179, 10.1007/s00203-002-0510-7.CrossRefGoogle ScholarPubMed
Díaz-Sánchez, J., Rosas-Aburto, A., Vivaldo-Lima, E., Hernández-Alcántara, J.M., Gracia-Mora, I., Vázquez-Torres, H., et al. 2017. Development and characterization of a flexible electrochromic device based on polyaniline and enzymatically synthesized poly (gallic acid). Synthetic Metals, 223, 10.1016/J.SYNTHMET.2016.11.038.CrossRefGoogle Scholar
Grass, G. & Rensing, C. 2001. Genes involved in copper homeostasis in Escherichia coli. Journal of Bacteriology, 183, 10.1128/JB.183.6.2145-2147.2001.CrossRefGoogle ScholarPubMed
Guan, Z.-B., Luo, Q., Wang, H.-R., Chen, Y. & Liao, X.-R. 2018. Bacterial laccases: promising biological green tools for industrial applications. Cellular and Molecular Life Sciences, 75, 10.1007/s00018-018-2883-z.CrossRefGoogle ScholarPubMed
Harkin, J.M., Larsen, M.J. & Obst, J.R. 1974. Use of syringaldazine for detection of laccase in sporophores of wood rotting fungi. Mycologia, 66, 10.2307/3758490.CrossRefGoogle ScholarPubMed
Jones, S.M. & Solomon, E.I. 2015. Electron transfer and reaction mechanism of laccases. Cellular and Molecular Life Sciences, 72, 10.1007/s00018-014-1826-6.CrossRefGoogle ScholarPubMed
Koschorreck, K., Richter, S.M., Ene, A.B., Roduner, E., Schmid, R.D. & Urlacher, V.B. 2008. Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids. Applied Microbiology and Biotechnology, 79, 10.1007/s00253-008-1417-2.CrossRefGoogle ScholarPubMed
Miyazaki, K. 2005. A hyperthermophilic laccase from Thermus thermophilus HB27. Extremophiles, 9, 10.1007/s00792-005-0458-z.CrossRefGoogle ScholarPubMed
Morozova, O.V., Shumakovich, G.P., Shleev, S.V. & Yaropolov, Ya.I. 2007. Laccase-mediator systems and their applications: a review. Applied Biochemistry and Microbiology, 43, 10.1134/S0003683807050055.CrossRefGoogle ScholarPubMed
Muñoz, P.A., Correa-Llantén, D.N. & Blamey, J.M. 2013. Production, purification and partial characterization of four lipases from a thermophile isolated from Deception Island. Lipids, 48, 10.1007/s11745-013-3771-9.CrossRefGoogle ScholarPubMed
Prajapati, H.V, Minocheherhomji, F.P. & Scholar, R. 2018. Laccase - a wonder molecule: a review of its properties and applications. International Journal of Pure and Applied Bioscience, 6, 10.18782/2320-7051.6233.CrossRefGoogle Scholar
Rowland, J.L. & Niederweis, M. 2013. A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis. Journal of Bacteriology, 195, 10.1128/JB.00546-13.CrossRefGoogle ScholarPubMed
Singh, G. & Arya, S.K. 2019. Utility of laccase in pulp and paper industry: a progressive step towards the green technology. International Journal of Biological Macromolecules, 134, 10.1016/j.ijbiomac.2019.05.168.CrossRefGoogle ScholarPubMed
Singh, R.L., Singh, P.K. & Singh, R.P. 2015. Enzymatic decolorization and degradation of azo dyes - a review. International Biodeterioration & Biodegradation, 104, 10.1016/J.IBIOD.2015.04.027.CrossRefGoogle Scholar
Verma, A. & Shirkot, P. 2014. Purification and characterization of thermostable laccase from Thermophilic Geobacillus thermocatenulatus MS5 and its applications in removal of textile dyes. Scholars Academic Journal of Biosciences Online, 2, 2321–6883.Google Scholar
Yang, J., Li, W., Ng, T.B., Deng, X., Lin, J. & Ye, X. 2017. Laccases: production, expression regulation, and applications in pharmaceutical biodegradation. Frontiers in Microbiology, 8, 10.3389/fmicb.2017.00832.Google Scholar
Yoshida, H. 1883. LXIII. - Chemistry of lacquer (Urushi). Part I. Communication from the Chemical Society of Tokio. Journal of the Chemical Society, Transactions, 43, 10.1039/CT8834300472.CrossRefGoogle Scholar