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Open AccessArticle

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

1
Centro de Investigaciones Biológicas (CSIC), C/Ramiro de Maeztu, 9, 28040 Madrid, Spain
2
Centro Nacional de Investigaciones Metalúrgicas (CSIC), C/Gregorio del Amo, 8, 28040 Madrid, Spain
*
Authors to whom correspondence should be addressed.
Academic Editor: Marco Filice
Molecules 2019, 24(7), 1313; https://doi.org/10.3390/molecules24071313
Received: 5 March 2019 / Revised: 29 March 2019 / Accepted: 2 April 2019 / Published: 3 April 2019
(This article belongs to the Special Issue Lipases and Lipases Modification 2019)
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. View Full-Text
Keywords: short-chain fatty acids esters; biocatalysis; recycling; green chemistry; fragrances; flavours short-chain fatty acids esters; biocatalysis; recycling; green chemistry; fragrances; flavours
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MDPI and ACS Style

Molina-Gutiérrez, M.; Hakalin, N.L.S.; Rodríguez-Sánchez, L.; Alcaraz, L.; López, F.A.; Martínez, M.J.; Prieto, A. Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae. Molecules 2019, 24, 1313. https://doi.org/10.3390/molecules24071313

AMA Style

Molina-Gutiérrez M, Hakalin NLS, Rodríguez-Sánchez L, Alcaraz L, López FA, Martínez MJ, Prieto A. Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae. Molecules. 2019; 24(7):1313. https://doi.org/10.3390/molecules24071313

Chicago/Turabian Style

Molina-Gutiérrez, María; Hakalin, Neumara L.S.; Rodríguez-Sánchez, Leonor; Alcaraz, Lorena; López, Félix A.; Martínez, María J.; Prieto, Alicia. 2019. "Effect of the Immobilization Strategy on the Efficiency and Recyclability of the Versatile Lipase from Ophiostoma piceae" Molecules 24, no. 7: 1313. https://doi.org/10.3390/molecules24071313

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