Ability of Ectoine to Stabilize Lipase against Elevated Temperatures and Methanol Concentrations

https://doi.org/10.22146/ijc.54931

I Putu Parwata(1), Deana Wahyuningrum(2), Sony Suhandono(3), Rukman Hertadi(4*)

(1) Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Bandung Institute of Technology, Jl. Ganesha No. 10, Bandung 40132, West Java, Indonesia Department of Analytical Chemistry, Faculty of Mathematics and Natural Sciences, Ganesha University of Education, Jl. Udayana No. 11, Bali 81116, Indonesia
(2) Organic Chemistry Research Division, Faculty of Mathematics and Natural Sciences, Bandung Institute of Technology, Jl. Ganesha No. 10, Bandung 40132, West Java, Indonesia
(3) Genetics and Molecular Biology Division, School of Biological Science and Technology, Bandung Institute of Technology, Jl. Ganesha No. 10, Bandung 40132, West Java, Indonesia
(4) Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Bandung Institute of Technology, Jl. Ganesha No. 10, Bandung 40132, West Java, Indonesia
(*) Corresponding Author

Abstract


Ectoine is one of the compatible organic molecules that can protect the protein from heating, freezing, and chemicals contact. This study aims to investigate the ability of ectoine to stabilize lipase on heating and in methanol treatments as an effort to provide a stable biocatalyst for the production of biodiesel. Various ectoine concentrations were added to lipase solutions, then the mixture was heated, and the residual activity of the lipase was determined. Similar steps were also conducted for methanol treatment. The results showed that ectoine maintained and even improved the catalytic activity of lipase after treatment with either heat or methanol. The addition of ectoine to a final concentration of 110 to 150 mM could maintain lipase activity up to 80% when heating to approximately 95 °C. Additionally, more than 20% of lipase activity increased on heating to temperatures below 75 °C in the presence of ectoine at a final concentration of 25 to 120 mM. Meanwhile, after incubation in methanol at a level of around 84% (v/v), the activity of lipase containing 40–90 mM ectoine was maintained. These results demonstrated that ectoine was highly effective in protecting lipase from heat and methanol.


Keywords


ectoine; lipase; heat; methanol; protection



References

[1] Chandra, P., Enespa, Singh, R., and Arora, P.K., 2020, Microbial lipases and their  industrial applications: A comprehensive review, Microb. Cell Fact., 19 (1), 169.

[2] Javed, S., Azeem, F., Hussain, S., Rasul, I., Siddique, M.H., Riaz, M., Afzal, M., Kouser, A., and Nadeem, H., 2018, Bacterial lipases: A review on purification and characterization, Prog. Biophys. Mol. Biol., 132, 23–34.

[3] Verma, N., Thakur, S., and Bhatt, A.K., 2012, Microbial lipases: Industrial applications and properties (A review), Int. Res. J. Biol. Sci., 1 (8), 88–92.

[4] Andualema, B., and Gessesse, A., 2012, Microbial lipases and their industrial applications: Review, Biotechnology, 11 (3), 100–118.

[5] Agobo, K.U., Arazu, V.A., Uzo, K., and Igwe, C.N., 2017, Microbial lipases: A prospect for biotechnological industrial catalysis for green products: A review, Ferment. Technol., 6 (2), 1000144.

[6] Salihu, A., and Alam, M.Z., 2014, Thermostable lipases: An overview of production, purification and characterization, Biosci. Biotechnol. Res. Asia, 11 (3), 1095–1107.

[7] Balan, A., Ibrahim, D., Rahim, R.A., and Rashid, A.A., 2012, Purification and characterization of a thermostable lipase from Geobacillus thermodenitrificans IBRL-nra, Enzyme Res., 2012, 987523.

[8] Aransiola, E.F., Ojumu, T.V., Oyekola, O.O., Madzimbamuto, T.F., and Ikhu-Omoregbe, D.I.O., 2014, A review of current technology for biodiesel production: State of the art, Biomass Bioenergy, 61, 276–297.

[9] Aghababaie, M., Beheshti, M., Bordbar, A.K., and Razmjou, A., 2018, Novel approaches to immobilize Candida rugose lipase on nanocomposite membranes prepared by covalent attachment of magnetic nanoparticles on poly acrylonitrile membrane, RSC Adv., 8 (9), 4561–4570.

[10] Ali, Z., Tian, L., Zhao, P., Zhang, B., Ali, N., Khan, M., and Zhang, Q., 2016, Immobilization of lipase on mesoporous silica nanoparticles with hierarchical fibrous pore, J. Mol. Catal. B: Enzym., 134, 129–135.

[11] Amirkhani, L., Moghaddas, J., and Jafarizadeh-Malmiri, H., 2016, Candida rugose lipase immobilization on magnetic silica aerogel nanodispersion, RSC Adv., 6 (15), 12676–12687.

[12] Badgujar, K.C., Dhake, K.P., and Bhanage, B.M., 2013, Immobilization of Candida cylindracea lipase on poly lactic acid, polyvinyl alcohol and chitosan based ternary blend film: Characterization, activity, stability and its application for N-acylation reactions, Process Biochem., 48 (9), 1335–1347.

[13] Brena, B., González-Pombo, P., and Batista-Viera, F., 2013, Immobilization of enzymes: A literature survey, Methods Mol. Biol., 1051, 15–31.

[14] Czech, L., Hermann, L., Stöveken, N., Richter, A.A., Höppner, A., Smits, S.H.J., Heider, J., and Bremer, E., 2018, Role of the extremolytes ectoine and hydroxyectoine as stress protectants and nutrients: Genetics, phylogenomics, biochemistry, and structural analysis, Genes, 9 (4), 177.

[15] Bakermans, C., 2015, Microbial Evolution under Extreme Conditions, De Gruyter, Berlin, Germany.

[16] Chamekh, R., Deniel, F., Donot, C., Jany, J.C., Nodet, P., and Belabid, L., 2019, Isolation, identification and enzymatic activity of halotolerant and halophilic fungi from the Great Sebkha of Oran in northwestern of Algeria, Mycobiology, 47 (2), 230–241.

[17] Chandrasekaran, M., 2016, Enzymes in Food and Beverage Processing, 1st Ed., CRC Press, Boca Raton, Florida, USA.

[18] Widderich, N., Höppner, A., Pittelkow, M., Heider, J., Smits, S.H., and Bremer, E., 2014, Biochemical properties of ectoine hydroxylases from extremophiles and their wider taxonomic distribution among microorganisms, PLoS ONE, 9 (4), e93809.

[19] Wang, Y., and Zhang, L., 2010, Ectoine improves yield of biodiesel catalyzed by immobilized lipase, J. Mol. Catal. B: Enzym., 62 (1), 90–95.

[20] Park, D.S., Oh, H.W., Heo, S.Y., Jeong, W.J., Shin, D.H., Bae, K.S., and Park, H.Y., 2007, Characterization of an extracellular lipase in Burkholderia sp. HY-10 isolated from a longicorn beetle, J. Microbiol., 45 (5), 409–417.

[21] Demirel, M., and Kayan, B., 2012, Application of response surface methodology and central composite design for the optimization of textile dye degradation by wet air oxidation, Int. J. Ind. Chem., 3 (1), 24.

[22] Dutka, M., Ditaranto, M., and Løvås, T., 2015, Application of a central composite design for the study of NOx emission performance of a low NOx burner, Energies, 8 (5), 3606–3627.

[23] Kunte, H.J., Lentzen, G., and Galinski, E.A., 2014, Industrial production of the cell protectant ectoine: Protection mechanisms, processes, and products, Curr. Biotechnol., 3 (1), 10–25.

[24] Mohammad, B.T., Al Daghistani, H.I., Jaouani, A., Abdel-Latif, S., and Kennes, C., 2017, Isolation and characterization of thermophilic bacteria from Jordanian hot springs: Bacillus licheniformis and Thermomonas hydrothermalis isolates as potential producers of thermostable enzymes, Int. J., Microbiol., 2017, 6943952.

[25] Bursy, J., Kuhlmann, A.U., Pittelkow, M., Hartmann, H., Jebbar, M., Pierik, A.J., and Bremer, E., 2008, Synthesis and uptake of the compatible solutes ectoine and 5-hydroxyectoine by Streptomyces coelicolor A3(2) in response to salt and heat stresses, Appl. Environ. Microbiol., 74 (23), 7286–7296.

[26] Piszkiewicz, S., and Pielak, G.J., 2019, Protecting enzymes from stress-induced inactivation, Biochemistry, 58 (37), 3825–3833.

[27] Bownik, A., and Stepniewska, Z., 2016, Ectoine as a promising protective agent in humans and animals, Arh. Hig. Rada Toksikol., 67, 260–265.

[28] Voet, D., and Voet, J.G., 2004, Biochemistry, 3rd Ed., John Wiley & Sons, New York.

[29] Subileau, M., Jan, A.H., Drone, J., Rutyna, C., Perrier, V., and Dubreucq, E., 2017, What makes a lipase a valuable acyltransferase in water abundant medium?, Catal. Sci. Technol., 7 (12), 2566–2578.



DOI: https://doi.org/10.22146/ijc.54931

Article Metrics

Abstract views : 122 | views : 153 | views : 56


Copyright (c) 2021 Indonesian Journal of Chemistry

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

 


Indonesian Journal of Chemistry (ISSN 1411-9420 / 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

Web
Analytics View The Statistics of Indones. J. Chem.