Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2
A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2...
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doaj-dc1f2f465fff4ff897d256ca13c2f7dd2021-09-05T13:59:43ZengSciendoPolish Journal of Chemical Technology1899-47412016-06-01182202510.1515/pjct-2016-0024pjct-2016-0024Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2Ozgen Melis0Attar Azade1Elalmis Yeliz2Birbir Meral3Yucel Sevil4Yildiz Technical University, Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Esenler, 34210 Istanbul, TurkeyYildiz Technical University, Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Esenler, 34210 Istanbul, TurkeyYildiz Technical University, Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Esenler, 34210 Istanbul, TurkeyMarmara University, Faculty of Science and Letters, Department of Biology, Goztepe, 34722 Istanbul, TurkeyYildiz Technical University, Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Esenler, 34210 Istanbul, TurkeyA strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2 were determined. It was observed that the lipolytic activity of Haloarcula hispanica was stimulated by some of the carbon sources. The high lipase acitivity values were obtained in the presence of 2% (v/v) walnut oil (6.16 U/ml), 1% (v/v) fish oil (5.07 U/ml), 1% (v/v) olive oil (4.52 U/ml) and 1% (w/v) stearic acid (4.88 U/ml) at 4M NaCl concentration. Lipase was partially purified by ammonium sulfate precipitation and ultrafiltration. Optimal temperature and pH values were determined as 45°C and 8.0, respectively. Lipase activity decreased with the increasing salt concentration, but 85% activity of the enzyme was maintained at 5M NaCl concentration. The enzyme preserved 41% of its relative activity at 90°C. The partially purified lipase maintained its activity in the presence of surfactants such as Triton X-100 and SDS. Therefore, the lipase which is an extremozyme may have potential applications especially in detergent industry.https://doi.org/10.1515/pjct-2016-0024haloarcula hispanicaextremely halophilic archaeaextremozymelipaselipolytic activity |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ozgen Melis Attar Azade Elalmis Yeliz Birbir Meral Yucel Sevil |
spellingShingle |
Ozgen Melis Attar Azade Elalmis Yeliz Birbir Meral Yucel Sevil Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 Polish Journal of Chemical Technology haloarcula hispanica extremely halophilic archaea extremozyme lipase lipolytic activity |
author_facet |
Ozgen Melis Attar Azade Elalmis Yeliz Birbir Meral Yucel Sevil |
author_sort |
Ozgen Melis |
title |
Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 |
title_short |
Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 |
title_full |
Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 |
title_fullStr |
Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 |
title_full_unstemmed |
Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2 |
title_sort |
enzymatic activity of a novel halotolerant lipase from haloarcula hispanica 2tk2 |
publisher |
Sciendo |
series |
Polish Journal of Chemical Technology |
issn |
1899-4741 |
publishDate |
2016-06-01 |
description |
A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2 were determined. It was observed that the lipolytic activity of Haloarcula hispanica was stimulated by some of the carbon sources. The high lipase acitivity values were obtained in the presence of 2% (v/v) walnut oil (6.16 U/ml), 1% (v/v) fish oil (5.07 U/ml), 1% (v/v) olive oil (4.52 U/ml) and 1% (w/v) stearic acid (4.88 U/ml) at 4M NaCl concentration. Lipase was partially purified by ammonium sulfate precipitation and ultrafiltration. Optimal temperature and pH values were determined as 45°C and 8.0, respectively. Lipase activity decreased with the increasing salt concentration, but 85% activity of the enzyme was maintained at 5M NaCl concentration. The enzyme preserved 41% of its relative activity at 90°C. The partially purified lipase maintained its activity in the presence of surfactants such as Triton X-100 and SDS. Therefore, the lipase which is an extremozyme may have potential applications especially in detergent industry. |
topic |
haloarcula hispanica extremely halophilic archaea extremozyme lipase lipolytic activity |
url |
https://doi.org/10.1515/pjct-2016-0024 |
work_keys_str_mv |
AT ozgenmelis enzymaticactivityofanovelhalotolerantlipasefromhaloarculahispanica2tk2 AT attarazade enzymaticactivityofanovelhalotolerantlipasefromhaloarculahispanica2tk2 AT elalmisyeliz enzymaticactivityofanovelhalotolerantlipasefromhaloarculahispanica2tk2 AT birbirmeral enzymaticactivityofanovelhalotolerantlipasefromhaloarculahispanica2tk2 AT yucelsevil enzymaticactivityofanovelhalotolerantlipasefromhaloarculahispanica2tk2 |
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