Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp.


  • Sezer Okay Hacettepe University
  • Şevki Adem Çankırı Karatekin University
  • Aslıhan Kurt-Kizildoğan Ondokuz Mayıs University



Archaeabacteria, Enzyme Stability, Halolamina, Lipase.


Enzymes of the archaea living in extreme environments are resistant to the challenging conditions. Lipase is among the important enzymes used in the industry and agriculture. In this study, the extracellular lipase from extremely halophilic archaeon Halolamina sp. was characterized for the first time. Optimum temperature for the enzyme activity was determined as 70oC, optimum pH was 7.0, and the optimum salt concentration was 3.6 M. Additionally, more than 70% of the enzyme activity was remained between pH 3.0-10.0 for 48 h as well as incubation of the enzyme at 70oC for 30 min increased its activity for 44%, and no activity loss was observed after incubation at 80oC. Also, presence of the metals increased the enzyme activity up to 88%. The enzyme was highly resistant to the organic solvents acetone, methanol, and DMSO while strong inhibition was caused by n-butanol. Among the detergents, the enzyme kept its activity substantially in the presence of SDS; however, other detergents caused inhibition of the enzyme activity. This characterization study showed that the lipase from the haloarchaeon Halolamina sp. is highly stable at the wide ranges of temperature and pH values as well as in the presence of diverse inhibitors. This enzyme is promising to be used in biotechnological applications.


Download data is not yet available.


ABANOZ, B., OKAY, S. and KURT-KIZILDOĞAN, A. Highly active and stable protease production by an extreme halophilic archaeon Haloarcula sp. TG1 isolated from Lake Tuz, Turkey. Turkish Journal of Biochemistry. 2017, 42(3), 307–315.

AMOOZEGAR, M.A., et al. Halophiles and their vast potential in biofuel production. Frontiers in Microbiology. 2019, 10, 1895.

AMOOZEGAR, M.A., et al. Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2. Journal of Basic Microbiology. 2008, 48(3), 160-167.

CASTILLA, A., et al. A novel thermophilic and halophilic esterase from Janibacter sp. R02, the first member of a new lipase family (Family XVII). Enzyme and Microbial Technology. 2017, 98, 86-95.

CORRAL, P., AMOOZEGAR, M.A. and VENTOSA, A. Halophiles and their biomolecules: Recent advances and future applications in biomedicine. Marine Drugs. 2020, 18(1), 33.

DASSARMA, S. and DASSARMA, P. Halophiles and their enzymes: negativity put to good use. Current Opinion in Microbiology. 2015, 25, 120-126.

DUMORNÉ, K., et al. Extremozymes: A potential source for industrial applications. Journal of Microbiology and Biotechnology. 2017, 27(4), 649-659.

EDBEIB, M.F., WAHAB, R.A. and HUYOP, F. Halophiles: biology, adaptation, and their role in decontamination of hypersaline environments. World Journal of Microbiology and Biotechnology. 2016, 32(8), 135.

ENACHE, M. and KAMEKURA, M. Hydrolytic enzymes of halophilic microorganisms and their economic values. Romanian Journal of Biochemistry. 2010, 47(1), 47–59.

FEBRIANI, et al. Novel thermostable lipase produced by a thermo-halophilic bacterium that catalyses hydrolytic and transesterification reactions. Heliyon. 2020, 6, e04520.

GUPTA, S., et al. Halophilic bacteria of Lunsu produce an array of industrially important enzymes with salt tolerant activity. Biochemistry Research International. 2016, 2016, 9237418.

KURT-KIZILDOĞAN, A., ABANOZ, B. and OKAY, S. Global transcriptome analysis of Halolamina sp. to decipher the salt tolerance in extremely halophilic archaea. Gene. 2017, 601, 56-64.

LAYE, V.J. and DASSARMA, S. An Antarctic extreme halophile and its polyextremophilic enzyme: Effects of perchlorate salts. Astrobiology. 2018, 18(4), 412-418.

LE, L.T.H.L., et al. Molecular characterization of a novel cold-active hormone-sensitive lipase (HaHSL) from Halocynthiibacter arcticus. Biomolecules. 2019, 9(11), 704.

LI, X. and YU, H.Y. Characterization of an organic solvent-tolerant lipase from Haloarcula sp. G41 and its application for biodiesel production. Folia Microbiologica (Praha). 2014, 59(6), 455-463.

LI, X., et al. Characterization of an organic solvent-tolerant lipase from Idiomarina sp. W33 and its application for biodiesel production using Jatropha oil. Extremophiles. 2014, 18(1), 171-178.

MALEKABADI, S., BADOEI-DALFARD, A. and KARAMI, Z. Biochemical characterization of a novel cold-active, halophilic and organic solvent-tolerant lipase from B. licheniformis KM12 with potential application for biodiesel production. International Journal of Biological Macromolecules. 2018, 109, 389-398.

MARTIN DEL CAMPO, M., et al. Solid-state fermentation as a potential technique for esterase/lipase production by halophilic archaea. Extremophiles. 2015, 19(6), 1121-1132.

MUSA, H., et al. Enhanced halophilic lipase secretion by Marinobacter litoralis SW-45 and its potential fatty acid esters release. Journal of Basic Microbiology. 2019, 59(1), 87-100.

OREN, A. Industrial and environmental applications of halophilic microorganisms. Environmental Technology. 2010, 31, 825-834.

OZCAN, B., et al. Characterization of extracellular esterase and lipase activities from five halophilic archaeal strains. Journal of Industrial Microbiology and Biotechnology. 2009, 36, 105-110.

PÉREZ, D., et al. A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA). PLoS One. 2011, 6, e23325.

RAJENDRAN, A. and THANGAVELU, V. Utilizing agricultural wastes as substrates for lipase production by Candida rugosa NCIM 3462 in solid-state fermentation: Response surface optimization of fermentation parameters. Waste and Biomass Valorization. 2013, 4, 347–357.

SAMAEI-NOUROOZI, A., et al. Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus. Extremophiles. 2015, 19, 933-947.

SANGEETHA, R., ARULPANDI, I. and GEETHA, A. Bacterial lipases as potential industrial biocatalysts: An overview. Research Journal of Microbiology. 2011, 6, 1-24.

SCHRECK, S.D. and GRUNDEN, A.M. Biotechnological applications of halophilic lipases and thioesterases. Applied Microbiology and Biotechnology. 2014, 98, 1011-1021.

SEHGAL, S.N. and GIBBONS, N.E. Effect of some metal ions on the growth of Halobacterium cutirubrum. Canadian Journal of Microbiology. 1960, 6, 165–169.

SHIVANAD, P., MUGERAYA, G. and KUMAR, A. Utilization of renewable agricultural residues for the production of extracellular halostable cellulase from newly isolated Halomonas sp. strain PS47. Annals of Microbiology. 2013, 63, 1257-1263.

SWAN, B.K., et al. Archaeal and bacterial communities respond differently to environmental gradients in anoxic sediments of a California hypersaline lake, the Salton Sea. Applied and Environmental Microbiology. 2010, 76, 757-768.

ŞAFAK, H., OTUR, Ç. and KURT-KIZILDOĞAN, A. Molecular and biochemical characterization of a recombinant endoglucanase rCKT3eng, from an extreme halophilic Haloarcula sp. strain CKT3. International Journal of Biological Macromolecules. 2020, 151, 1173–1180.

WADITEE-SIRISATTHA, R., KAGEYAMA, H. and TAKABE, T. Halophilic microorganism resources and their applications in industrial and environmental biotechnology. AIMS Microbiology. 2016, 2, 42-54.

WOODLEY, J.M., BREUER, M. and MINK, D. A future perspective on the role of industrial biotechnology for chemicals production. Chemical Engineering Research and Design. 2013, 91(10), 2029–2036.




How to Cite

OKAY, S., ADEM, Şevki and ASLIHAN KURT-KIZILDOĞAN, 2022. Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. Bioscience Journal [online], vol. 38, pp. e38039. [Accessed12 August 2022]. DOI 10.14393/BJ-v38n0a2022-53865. Available from:



Biological Sciences