<abstract xmlns="http://www.w3.org/1999/xhtml"><p>A strain of <italic>Haloarcula hispanica</italic> 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 <italic>Haloarcula hispanica</italic> 2TK2 were determined. It was observed that the lipolytic activity of <italic>Haloarcula hispanica</italic> 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.</p></abstract>

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.

Enzymatic activity of a novel halotolerant lipase from <italic>Haloarcula hispanica</italic> 2TK2

Yildiz Technical University, Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Esenler, 34210 Istanbul, Turkey

Marmara University, Faculty of Science and Letters, Department of Biology, Goztepe, 34722 Istanbul, Turkey

Polish Journal of Chemical Technology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Enzymatic activity of a novel halotolerant lipase from  2TK2

A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources...

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

Pubblicato online: 30 giu 2016

Pagine: 20 - 25

DOI: https://doi.org/10.1515/pjct-2016-0024

Parole chiave
extremely halophilic archaea, extremozyme, lipase, lipolytic activity

© 2016 Melis Ozgen et al., published by De Gruyter Open

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

Pubblicato online: 30 giu 2016

Pagine: 20 - 25

DOI: https://doi.org/10.1515/pjct-2016-0024

Parole chiaveextremely halophilic archaea, extremozyme, lipase, lipolytic activity

© 2016 Melis Ozgen et al., published by De Gruyter Open

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Parole chiave
extremely halophilic archaea, extremozyme, lipase, lipolytic activity