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Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae

The recombinant lipase from Ophiostoma piceae OPEr has demonstrated to have catalytic properties superior to those of many commercial enzymes. Enzymatic crudes with OPEr were immobilized onto magnetite nanoparticles by hydrophobicity (SiMAG-Octyl) and by two procedures that involve covalent attachme...

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Autores principales: Molina-Gutiérrez, María, Hakalin, Neumara L. S., Rodríguez-Sánchez, Leonor, Alcaraz, Lorena, López, Félix A., Martínez, María Jesús, Prieto, Alicia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480004/
https://www.ncbi.nlm.nih.gov/pubmed/30987194
http://dx.doi.org/10.3390/molecules24071313
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author Molina-Gutiérrez, María
Hakalin, Neumara L. S.
Rodríguez-Sánchez, Leonor
Alcaraz, Lorena
López, Félix A.
Martínez, María Jesús
Prieto, Alicia
author_facet Molina-Gutiérrez, María
Hakalin, Neumara L. S.
Rodríguez-Sánchez, Leonor
Alcaraz, Lorena
López, Félix A.
Martínez, María Jesús
Prieto, Alicia
author_sort Molina-Gutiérrez, María
collection PubMed
description The recombinant lipase from Ophiostoma piceae OPEr has demonstrated to have catalytic properties superior to those of many commercial enzymes. Enzymatic crudes with OPEr were immobilized onto magnetite nanoparticles by hydrophobicity (SiMAG-Octyl) and by two procedures that involve covalent attachment of the protein (mCLEAs and AMNP-GA), giving three nanobiocatalysts with different specific activity in hydrolysis of p-nitrophenyl butyrate (pNPB) and good storage stability at 4 °C over a period of 4 months. Free OPEr and the different nanobiocatalysts were compared for the synthesis of butyl esters of volatile fatty acids C4 to C7 in reactions containing the same lipase activity. The esterification yields and the reaction rates obtained with AMNP-GA-OPEr were in general higher or similar to those observed for the free enzyme, the mCLEAs-OPEr, and the non-covalent preparation SiMAG-Octyl-OPEr. The time course of the esterification of the acids C4 to C6 catalyzed by AMNP-GA-OPEr was comparable. The synthesis of the C7 ester was slower but very efficient, admitting concentrations of heptanoic acid up to 1 M. The best 1-butanol: acid molar ratio was 2:1 for all the acids tested. Depending on the substrate, this covalent preparation of OPEr maintained 80–96% activity over 7 cycles, revealing its excellent properties, easy recovery and recycling, and its potential to catalyze the green synthesis of chemicals of industrial interest.
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spelling pubmed-64800042019-04-30 Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae Molina-Gutiérrez, María Hakalin, Neumara L. S. Rodríguez-Sánchez, Leonor Alcaraz, Lorena López, Félix A. Martínez, María Jesús Prieto, Alicia Molecules Article The recombinant lipase from Ophiostoma piceae OPEr has demonstrated to have catalytic properties superior to those of many commercial enzymes. Enzymatic crudes with OPEr were immobilized onto magnetite nanoparticles by hydrophobicity (SiMAG-Octyl) and by two procedures that involve covalent attachment of the protein (mCLEAs and AMNP-GA), giving three nanobiocatalysts with different specific activity in hydrolysis of p-nitrophenyl butyrate (pNPB) and good storage stability at 4 °C over a period of 4 months. Free OPEr and the different nanobiocatalysts were compared for the synthesis of butyl esters of volatile fatty acids C4 to C7 in reactions containing the same lipase activity. The esterification yields and the reaction rates obtained with AMNP-GA-OPEr were in general higher or similar to those observed for the free enzyme, the mCLEAs-OPEr, and the non-covalent preparation SiMAG-Octyl-OPEr. The time course of the esterification of the acids C4 to C6 catalyzed by AMNP-GA-OPEr was comparable. The synthesis of the C7 ester was slower but very efficient, admitting concentrations of heptanoic acid up to 1 M. The best 1-butanol: acid molar ratio was 2:1 for all the acids tested. Depending on the substrate, this covalent preparation of OPEr maintained 80–96% activity over 7 cycles, revealing its excellent properties, easy recovery and recycling, and its potential to catalyze the green synthesis of chemicals of industrial interest. MDPI 2019-04-03 /pmc/articles/PMC6480004/ /pubmed/30987194 http://dx.doi.org/10.3390/molecules24071313 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Molina-Gutiérrez, María
Hakalin, Neumara L. S.
Rodríguez-Sánchez, Leonor
Alcaraz, Lorena
López, Félix A.
Martínez, María Jesús
Prieto, Alicia
Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title_full Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title_fullStr Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title_full_unstemmed Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title_short Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae
title_sort effect of the immobilization strategy on the efficiency and recyclability of the versatile lipase from ophiostoma piceae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480004/
https://www.ncbi.nlm.nih.gov/pubmed/30987194
http://dx.doi.org/10.3390/molecules24071313
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