Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate

With green technologies, the damages caused by agro-technological wastes to the environment are eliminated. In our study, it was aimed both to prevent the harm of olive oil waste to the environment and to produce lipase enzyme, which is an important biotechnological product.. E. faecium E68 obtained...

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Autores principales: KIVANC, merih, Acu, Esra
Formato: Online
Lenguaje:eng
Publicado: Universidad de Sonora 2022
Acceso en línea:https://biotecnia.unison.mx/index.php/biotecnia/article/view/1750
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spelling biotecnia-article-17502022-10-28T15:06:34Z Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate Producción de lipasa extracelular por Enterococcus faecium E68 en residuos de aceite de oliva como sustrato KIVANC, merih Acu, Esra Enterococcus faecium, Lipase activity, Olive oil waste, lipase Enterococcus faecium actividad de lipasa residuos de aceite de oliva lipasa With green technologies, the damages caused by agro-technological wastes to the environment are eliminated. In our study, it was aimed both to prevent the harm of olive oil waste to the environment and to produce lipase enzyme, which is an important biotechnological product.. E. faecium E68 obtained from milk and dairy products was used in the production of lipase enzyme. E. faecium E68 was developed in lipase production medium containing 10% olive waste, pH6.5, at 37oC with 120 rpm agitation for 48 hours. The effect of temperature, pH metal ion, surfactant and NaCl was also determined. The molecular weight of the partially purified extracellular lipase enzyme was estimated to be around 19-20 kDa  by SDS-PAGE.   The optimum temperature was 45°C, while the enzyme exhibited appreciable thermostability retaining of activity at 55°C for 48h. The lipase was most active in the pH range of 3-11 with an optimum activity at pH 10. 1mM, Ca 2+, Mn2+, Cu2+, Ni2+, Zn2+, Mg2+ and K+ ions modulated the activity of the enzyme but inhibited by Hg2+, SDS and Triton X-100. The enzyme is halophilic and 25% NaCl salt increased the activity. Olive oil waste may be the preferred substrate for lipase production. Con las tecnologías verdes se eliminan los daños que ocasionan los desechos agrotecnológicos al medio ambiente. En nuestro estudio, el objetivo era prevenir el daño de los residuos de aceite de oliva al medio ambiente y producir la enzima lipasa, que es un producto biotecnológico importante. E. faecium E68 obtenido de leche y productos lácteos se utilizó en la producción de la enzima lipasa. E. faeciumE68 se desarrolló en medio de producción de lipasa con un 10% de orujo de aceituna, pH 6,5, a 37 oC con agitación a 120 rpm durante 48 h. También se determinó el efecto de la temperatura, el pH del ion metálico, el surfactante y el NaCl. El peso molecular de la enzima lipasa extracelular parcialmente purificada se estimó en alrededor de 19-20 kDa mediante SDS-PAGE. La temperatura óptima fue de 45 °C, mientras que la enzima exhibió una termoestabilidad apreciable reteniendo la actividad a 55°C durante 48 h. La actividad óptima de la lipasa fue a pH10. Los iones 1mM, Ca 2+, Mn2+, Cu2+, Ni2+, Zn2+, Mg2+ y K+ modularon la actividad de la enzima pero fueron inhibidos por Hg2+, SDS y Triton X-100. La enzima es halófila y la sal de NaCl al 25% aumentó la actividad. Universidad de Sonora 2022-10-06 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Original peer-reviewed articles Artículos originales evaluados por pares application/pdf https://biotecnia.unison.mx/index.php/biotecnia/article/view/1750 10.18633/biotecnia.v24i3.1750 Biotecnia; Vol. 24 No. 3 (2022): Septiembre-Diciembre; 87-93 Biotecnia; Vol. 24 Núm. 3 (2022): Septiembre-Diciembre; 87-93 1665-1456 1665-1456 eng https://biotecnia.unison.mx/index.php/biotecnia/article/view/1750/711 Derechos de autor 2022 https://creativecommons.org/licenses/by-nc-sa/4.0
institution Biotecnia
collection OJS
language eng
format Online
author KIVANC, merih
Acu, Esra
spellingShingle KIVANC, merih
Acu, Esra
Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
author_facet KIVANC, merih
Acu, Esra
author_sort KIVANC, merih
title Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
title_short Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
title_full Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
title_fullStr Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
title_full_unstemmed Production of extracellular lipase by Enterococcus faecium E68 with olive oil waste as substrate
title_sort production of extracellular lipase by enterococcus faecium e68 with olive oil waste as substrate
description With green technologies, the damages caused by agro-technological wastes to the environment are eliminated. In our study, it was aimed both to prevent the harm of olive oil waste to the environment and to produce lipase enzyme, which is an important biotechnological product.. E. faecium E68 obtained from milk and dairy products was used in the production of lipase enzyme. E. faecium E68 was developed in lipase production medium containing 10% olive waste, pH6.5, at 37oC with 120 rpm agitation for 48 hours. The effect of temperature, pH metal ion, surfactant and NaCl was also determined. The molecular weight of the partially purified extracellular lipase enzyme was estimated to be around 19-20 kDa  by SDS-PAGE.   The optimum temperature was 45°C, while the enzyme exhibited appreciable thermostability retaining of activity at 55°C for 48h. The lipase was most active in the pH range of 3-11 with an optimum activity at pH 10. 1mM, Ca 2+, Mn2+, Cu2+, Ni2+, Zn2+, Mg2+ and K+ ions modulated the activity of the enzyme but inhibited by Hg2+, SDS and Triton X-100. The enzyme is halophilic and 25% NaCl salt increased the activity. Olive oil waste may be the preferred substrate for lipase production.
publisher Universidad de Sonora
publishDate 2022
url https://biotecnia.unison.mx/index.php/biotecnia/article/view/1750
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