Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp.
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 tim...
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| Format: | Article |
| Language: | English |
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Universidade Federal de Uberlândia
2022-08-01
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| Series: | Bioscience Journal |
| Subjects: | |
| Online Access: | https://seer.ufu.br/index.php/biosciencejournal/article/view/53865 |
| _version_ | 1798038671697379328 |
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| author | Sezer Okay Şevki Adem Aslıhan Kurt-Kizildoğan |
| author_facet | Sezer Okay Şevki Adem Aslıhan Kurt-Kizildoğan |
| author_sort | Sezer Okay |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T21:43:23Z |
| format | Article |
| id | doaj.art-c6a2eb621ea34911914fd1bcdaa4df12 |
| institution | Directory Open Access Journal |
| issn | 1981-3163 |
| language | English |
| last_indexed | 2024-04-11T21:43:23Z |
| publishDate | 2022-08-01 |
| publisher | Universidade Federal de Uberlândia |
| record_format | Article |
| series | Bioscience Journal |
| spelling | doaj.art-c6a2eb621ea34911914fd1bcdaa4df122022-12-22T04:01:31ZengUniversidade Federal de UberlândiaBioscience Journal1981-31632022-08-0138e38039e3803910.14393/BJ-v38n0a2022-5386528038Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp.Sezer Okay0Şevki Adem1Aslıhan Kurt-Kizildoğan2https://orcid.org/0000-0002-9323-0993Hacettepe UniversityÇankırı Karatekin UniversityOndokuz Mayıs UniversityEnzymes 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.https://seer.ufu.br/index.php/biosciencejournal/article/view/53865archaeabacteriaenzyme stabilityhalolaminalipase. |
| spellingShingle | Sezer Okay Şevki Adem Aslıhan Kurt-Kizildoğan Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. Bioscience Journal archaeabacteria enzyme stability halolamina lipase. |
| title | Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
| title_full | Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
| title_fullStr | Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
| title_full_unstemmed | Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
| title_short | Characterization of highly stable extracellular lipase from the extremely halophilic archaeon Halolamina sp. |
| title_sort | characterization of highly stable extracellular lipase from the extremely halophilic archaeon halolamina sp |
| topic | archaeabacteria enzyme stability halolamina lipase. |
| url | https://seer.ufu.br/index.php/biosciencejournal/article/view/53865 |
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