A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).

<h4>Background</h4>Among extremophiles, halophiles are defined as microorganisms adapted to live and thrive in diverse extreme saline environments. These extremophilic microorganisms constitute the source of a number of hydrolases with great biotechnological applications. The interest to...

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Autores principales:	Dolores Pérez, Sara Martín, Gloria Fernández-Lorente, Marco Filice, José Manuel Guisán, Antonio Ventosa, María Teresa García, Encarnación Mellado
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/19111e8828884162b319b2ce146f069a
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spelling	oai:doaj.org-article:19111e8828884162b319b2ce146f069a2021-11-18T06:48:18ZA novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).1932-620310.1371/journal.pone.0023325https://doaj.org/article/19111e8828884162b319b2ce146f069a2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21853111/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Among extremophiles, halophiles are defined as microorganisms adapted to live and thrive in diverse extreme saline environments. These extremophilic microorganisms constitute the source of a number of hydrolases with great biotechnological applications. The interest to use extremozymes from halophiles in industrial applications is their resistance to organic solvents and extreme temperatures. Marinobacter lipolyticus SM19 is a moderately halophilic bacterium, isolated previously from a saline habitat in South Spain, showing lipolytic activity.<h4>Methods and findings</h4>A lipolytic enzyme from the halophilic bacterium Marinobacter lipolyticus SM19 was isolated. This enzyme, designated LipBL, was expressed in Escherichia coli. LipBL is a protein of 404 amino acids with a molecular mass of 45.3 kDa and high identity to class C β-lactamases. LipBL was purified and biochemically characterized. The temperature for its maximal activity was 80°C and the pH optimum determined at 25°C was 7.0, showing optimal activity without sodium chloride, while maintaining 20% activity in a wide range of NaCl concentrations. This enzyme exhibited high activity against short-medium length acyl chain substrates, although it also hydrolyzes olive oil and fish oil. The fish oil hydrolysis using LipBL results in an enrichment of free eicosapentaenoic acid (EPA), but not docosahexaenoic acid (DHA), relative to its levels present in fish oil. For improving the stability and to be used in industrial processes LipBL was immobilized in different supports. The immobilized derivatives CNBr-activated Sepharose were highly selective towards the release of EPA versus DHA. The enzyme is also active towards different chiral and prochiral esters. Exposure of LipBL to buffer-solvent mixtures showed that the enzyme had remarkable activity and stability in all organic solvents tested.<h4>Conclusions</h4>In this study we isolated, purified, biochemically characterized and immobilized a lipolytic enzyme from a halophilic bacterium M. lipolyticus, which constitutes an enzyme with excellent properties to be used in the food industry, in the enrichment in omega-3 PUFAs.Dolores PérezSara MartínGloria Fernández-LorenteMarco FiliceJosé Manuel GuisánAntonio VentosaMaría Teresa GarcíaEncarnación MelladoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 8, p e23325 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Dolores Pérez Sara Martín Gloria Fernández-Lorente Marco Filice José Manuel Guisán Antonio Ventosa María Teresa García Encarnación Mellado A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
description	<h4>Background</h4>Among extremophiles, halophiles are defined as microorganisms adapted to live and thrive in diverse extreme saline environments. These extremophilic microorganisms constitute the source of a number of hydrolases with great biotechnological applications. The interest to use extremozymes from halophiles in industrial applications is their resistance to organic solvents and extreme temperatures. Marinobacter lipolyticus SM19 is a moderately halophilic bacterium, isolated previously from a saline habitat in South Spain, showing lipolytic activity.<h4>Methods and findings</h4>A lipolytic enzyme from the halophilic bacterium Marinobacter lipolyticus SM19 was isolated. This enzyme, designated LipBL, was expressed in Escherichia coli. LipBL is a protein of 404 amino acids with a molecular mass of 45.3 kDa and high identity to class C β-lactamases. LipBL was purified and biochemically characterized. The temperature for its maximal activity was 80°C and the pH optimum determined at 25°C was 7.0, showing optimal activity without sodium chloride, while maintaining 20% activity in a wide range of NaCl concentrations. This enzyme exhibited high activity against short-medium length acyl chain substrates, although it also hydrolyzes olive oil and fish oil. The fish oil hydrolysis using LipBL results in an enrichment of free eicosapentaenoic acid (EPA), but not docosahexaenoic acid (DHA), relative to its levels present in fish oil. For improving the stability and to be used in industrial processes LipBL was immobilized in different supports. The immobilized derivatives CNBr-activated Sepharose were highly selective towards the release of EPA versus DHA. The enzyme is also active towards different chiral and prochiral esters. Exposure of LipBL to buffer-solvent mixtures showed that the enzyme had remarkable activity and stability in all organic solvents tested.<h4>Conclusions</h4>In this study we isolated, purified, biochemically characterized and immobilized a lipolytic enzyme from a halophilic bacterium M. lipolyticus, which constitutes an enzyme with excellent properties to be used in the food industry, in the enrichment in omega-3 PUFAs.
format	article
author	Dolores Pérez Sara Martín Gloria Fernández-Lorente Marco Filice José Manuel Guisán Antonio Ventosa María Teresa García Encarnación Mellado
author_facet	Dolores Pérez Sara Martín Gloria Fernández-Lorente Marco Filice José Manuel Guisán Antonio Ventosa María Teresa García Encarnación Mellado
author_sort	Dolores Pérez
title	A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
title_short	A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
title_full	A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
title_fullStr	A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
title_full_unstemmed	A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).
title_sort	novel halophilic lipase, lipbl, showing high efficiency in the production of eicosapentaenoic acid (epa).
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/19111e8828884162b319b2ce146f069a
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A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA).

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