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

Authors

  • Sezer Okay Hacettepe University
  • Şevki Adem Çankırı Karatekin University
  • Aslıhan Kurt-Kizildoğan Ondokuz Mayıs University https://orcid.org/0000-0002-9323-0993

DOI:

https://doi.org/10.14393/BJ-v38n0a2022-53865

Keywords:

Archaeabacteria, Enzyme Stability, Halolamina, Lipase.

Abstract

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.

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References

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Published

2022-08-05

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: https://seer.ufu.br/index.php/biosciencejournal/article/view/53865.

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Section

Biological Sciences