Thermostability and functionality evaluation of laccases from Pleurotus ostreatus and Pycnoporus cinnabarinus: An In-silico assay Biochemical properties of laccases from fungi in silico method
Iranian Journal of Pharmaceutical Sciences,
Vol. 19 No. 2 (2023),
1 April 2023
,
Page 88-98
https://doi.org/10.22037/ijps.v19i2.42246
Abstract
Laccase enzymes are widely used in industrials and therefore achievement to the resources of this enzyme with high thermostability is obligatory. Accordingly, a deeper investigation for understanding the structure and function of PoxA1b from Pleurotus ostreatus, as a fungal enzyme with the possible desired conditions, was accomplished by using in-silico methods. Our study led to modeling a tertiary structure of the enzyme with 72% identity to the laccase from Trametes sp. AH28-2, with high quality. Moreover, structural stability of modeled enzyme compared to laccase from Pycnoporus cinnabarinus (LPC), were proved during 20 ns at 300 and 333K. Interestingly, this data showed that the modeled enzyme is more stable than LPC at 333 K. On the other hand, interaction assay of PoxA1b and LPC with benzo[a]pyrene (BaP), as a Polycyclic aromatic hydrocarbons (PAHs), revealed suitable affinity for both of them with -9.1 and -8.8 of binding energy, respectively. Taken together, these data show that both laccase from Pleurotus ostreatus and Pycnoporus cinnabarinus are stable until 60 °C with suitable affinity to substrate. Bearing in mind, PoxA1b is a favorable candidate for industrial and environmental applications, especially in PAH detoxification.
- Enzyme activity
- PoxA1b
- Stability
- PAHs
- Molecular simulation
How to Cite
References
Nunes, C.S. and A. Kunamneni, Laccases—properties and applications, in Enzymes in human and animal nutrition. 2018, Elsevier. p. 133-161.
Chowdhary, P., et al., Microbial manganese peroxidase: a ligninolytic enzyme and its ample opportunities in research. 2019. 1: p. 1-12.
Christensen, N.J. and K.P. Kepp, Stability mechanisms of a thermophilic laccase probed by molecular dynamics. PloS one, 2013. 8(4): p. e61985.
Zimbardi, A.L., et al., A High Redox Potential Laccase from Pycnoporus sanguineus RP15: Potential Application for Dye Decolorization. International journal of molecular sciences, 2016. 17(5): p. 672.
Rivera-Hoyos, C.M., et al., Computational analysis and low-scale constitutive expression of laccases synthetic genes GlLCC1 from Ganoderma lucidum and POXA 1B from Pleurotus ostreatus in Pichia pastoris. PloS one, 2015. 10(1): p. e0116524.
IMRAN, M., et al., Production and industrial applications of laccase enzyme. Journal of Cell & Molecular Biology, 2012. 10(1).
Välimets, S., et al., Secretory expression of recombinant small laccase genes in Gram-positive bacteria. Microbial Cell Factories, 2023. 22(1): p. 1-14.
Sondhi, S., et al., Laccase: A Green Solution for Environmental Problems. Advances in Environmental and Engineering Research, 2023. 4(2): p. 1-32.
Ekeoma, B.C., et al., Recent Advances in the Biocatalytic Mitigation of Emerging Pollutants: A Comprehensive Review. Journal of Biotechnology, 2023.
Mishra, A., S. Kumar, and A.J.M.W.T. Bhatnagar, Potential of fungal laccase in decolorization of synthetic dyes. 2019: p. 127-151.
Moghimi, H., et al., Assessing the biodegradation of polycyclic aromatic hydrocarbons and laccase production by new fungus Trematophoma sp. UTMC 5003. 2017. 33: p. 1-10.
Mtibaà, R., et al., Degradation of bisphenol A and acute toxicity reduction by different thermo-tolerant ascomycete strains isolated from arid soils. 2018. 156: p. 87-96.
Hildén, K., T.K. Hakala, and T. Lundell, Thermotolerant and thermostable laccases. Biotechnology letters, 2009. 31(8): p. 1117.
Aza, P., et al., Protein engineering approaches to enhance fungal laccase production in S. cerevisiae. 2021. 22(3): p. 1157.
El-Batal, A.I., et al., Laccase production by Pleurotus ostreatus and its application in synthesis of gold nanoparticles. Biotechnology Reports, 2015. 5: p. 31-39.
Faheem, M., et al., Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5. Folia Microbiologica, 2023: p. 1-22.
Alves, A.M., et al., Highly efficient production of laccase by the basidiomycete Pycnoporus cinnabarinus. Applied and Environmental Microbiology, 2004. 70(11): p. 6379-6384.
Ren, Y., et al., A green process for flax fiber extraction by white rot fungus (Laccase mediators system) in a less-water environment. Industrial Crops and Products, 2023. 193: p. 116209.
El Enshasy, H., et al., Pleurotus ostreatus: A biofactory for lignin-degrading enzymes of diverse industrial applications. Recent Advancement in White Biotechnology Through Fungi: Volume 3: Perspective for Sustainable Environments, 2019: p. 101-152.
Macellaro, G., et al., Effective mutations in a high redox potential laccase from Pleurotus ostreatus. Applied microbiology and biotechnology, 2014. 98(11): p. 4949-4961.
Othman, A.M., et al., Purification, biochemical characterization and applications of Pleurotus ostreatus ARC280 Laccase. British Microbiology Research Journal, 2014. 4(12): p. 1418-1439.
Upadhyay, P., R. Shrivastava, and P.K. Agrawal, Bioprospecting and biotechnological applications of fungal laccase. 3 Biotech, 2016. 6(1): p. 1-12.
Jamshidi, Z., M. Akaberi, and F. Hadizadeh, In silico study of five SARS CoV-2 target proteins on known drugs. Iranian Journal of Pharmaceutical Sciences, 2021. 17(2): p. 87-104.
Yasman, S., et al., In Silico Analysis of Sea Cucumber Bioactive Compounds as Anti-Breast Cancer Mechanism Using AutoDock Vina. Iranian Journal of Pharmaceutical Sciences, 2020. 16(1): p. 1-8.
Maximova, T., et al., Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics. PLoS Comput Biol, 2016. 12(4): p. e1004619.
Piontek, K., et al., Substrate Binding and Copper Geometry in Laccases. (To Be Published), 2010.
Ge, H., et al., Structure of native laccase B from Trametes sp. AH28-2. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010. 66(Pt 3): p. 254-8.
Magnan, C.N. and P.J.B. Baldi, SSpro/ACCpro 5: almost perfect prediction of protein secondary structure and relative solvent accessibility using profiles, machine learning and structural similarity. 2014. 30(18): p. 2592-2597.
Webb, B. and A. Sali, Comparative Protein Structure Modeling Using MODELLER. Curr Protoc Protein Sci, 2016. 86: p. 2 9 1-2 9 37.
Lovell, S.C., et al., Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins: Structure, Function & Genetics, 2002. 50: p. 437-450.
Hess, B., et al., LINCS: A linear constraint solver for molecular simulations. Journal of Computational Chemistry, 1997. 18(12): p. 1463-1472.
Talebi, H., et al., Molecular dynamics/XFEM coupling by a three-dimensional extended bridging domain with applications to dynamic brittle fracture. 2013. 11(6).
Ahmed, R.S., et al., Assessment of environmental and toxicity impacts and potential health hazards of heavy metals pollution of agricultural drainage adjacent to industrial zones in Egypt. Chemosphere, 2023. 318: p. 137872.
Taghavizadeh Yazdi, M.E., et al., Bio-indicators in cadmium toxicity: Role of HSP27 and HSP70. Environmental Science and Pollution Research, 2021. 28(21): p. 26359-26379.
Sepahi, S., et al., Biochemical responses as early and reliable biomarkers of organophosphate and carbamate pesticides intoxication: A systematic literature review. Journal of Biochemical and Molecular Toxicology, 2022: p. e23285.
Thacharodi, A., et al., Bioremediation of polycyclic aromatic hydrocarbons: An updated microbiological review. Chemosphere, 2023: p. 138498.
Patel, A.B., et al., Polycyclic aromatic hydrocarbons: sources, toxicity, and remediation approaches. 2020. 11: p. 562813.
Narayanan, M., S.S. Ali, and M. El-Sheekh, A comprehensive review on the potential of microbial enzymes in multipollutant bioremediation: Mechanisms, challenges, and future prospects. Journal of Environmental Management, 2023. 334: p. 117532.
Nagatani, A., A. Mokhtar, and T. Okobira, A highly efficient laccase-immobilized bioreactor prepared by radiation induced graft polymerization for removal of persistent pollutants. Bioresource Technology Reports, 2023: p. 101444.
Ibarra, D., et al., Exploring the enzymatic parameters for optimal delignification of eucalypt pulp by laccase-mediator. Enzyme and microbial technology, 2006. 39(6): p. 1319-1327.
Bangoria, P., A. Patel, and A.R. Shah, Thermotolerant and protease-resistant GH5 family β-mannanase with CBM1 from Penicillium aculeatum APS1: purification and characterization. 3 Biotech, 2023. 13(3): p. 107.
Viswanath, B., et al., Fungal laccases and their applications in bioremediation. Enzyme research, 2014. 2014.
Gałązka, A., U. Jankiewicz, and A. Szczepkowski, Biochemical Characteristics of Laccases and Their Practical Application in the Removal of Xenobiotics from Water. Applied Sciences, 2023. 13(7): p. 4394.
Record, E., et al., Expression of the Pycnoporus cinnabarinus laccase gene in Aspergillus niger and characterization of the recombinant enzyme. European Journal of Biochemistry, 2002. 269(2): p. 602-609.
Garcia, T.A., M.F. Santiago, and C.J. Ulhoa, Studies on the Pycnoporus sanguineus CCT-4518 laccase purified by hydrophobic interaction chromatography. Applied microbiology and biotechnology, 2007. 75(2): p. 311-318.
Schliephake, K., et al., Transformation and degradation of the disazo dye Chicago Sky Blue by a purified laccase from Pycnoporus cinnabarinus. Enzyme and microbial technology, 2000. 27(1): p. 100-107.
Mahuri, M., M. Paul, and H. Thatoi, A review of microbial laccase production and activity toward different biotechnological applications. Systems Microbiology and Biomanufacturing, 2023: p. 1-19.
Hasan, S., et al., Laccase production from local biomass using solid state fermentation. Fermentation, 2023. 9(2): p. 179.
Palmieri, G., et al., A novel white laccase from Pleurotus ostreatus. Journal of Biological Chemistry, 1997. 272(50): p. 31301-31307.
Jordaan, J., B. Pletschke, and W. Leukes, Purification and partial characterization of a thermostable laccase from an unidentified basidiomycete. Enzyme and microbial technology, 2004. 34(7): p. 635-641.
Battaglia, V., et al., Potential Use of Cardunculus Biomass on Pleurotus eryngii Production: Heteroglycans Content and Nutritional Properties (Preliminary Results). Foods, 2023. 12(1): p. 58.
Giardina, P., et al., Protein and gene structure of a blue laccase from Pleurotus ostreatus1. Biochemical Journal, 1999. 341(3): p. 655-663.
Eggert, C., U. Temp, and K.-E. Eriksson, The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Applied and Environmental Microbiology, 1996. 62(4): p. 1151-1158.
Pakhadnia, Y., N. Malinouski, and A. Lapko, Purification and characteristics of an enzyme with both bilirubin oxidase and laccase activities from mycelium of the basidiomycete Pleurotus ostreatus. Biochemistry (Moscow), 2009. 74(9): p. 1027-1034.
Patel, H., et al., Purification and characterization of an extracellular laccase from solid-state culture of Pleurotus ostreatus HP-1. 3 Biotech, 2014. 4(1): p. 77-84.
Lahtinen, M., et al., The effect of lignin model compound structure on the rate of oxidation catalyzed by two different fungal laccases. Journal of Molecular Catalysis B: Enzymatic, 2009. 57(1): p. 204-210.
Chen, M., et al., Understanding lignin-degrading reactions of ligninolytic enzymes: binding affinity and interactional profile. PLoS One, 2011. 6(9): p. e25647
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