Cargando…

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

In this communication, it was evaluated the production of fatty acid ethyl ester (FAAE) from the free fatty acids of babassu oil catalyzed by lipase from Rhizomucor miehei (RML) immobilized on magnetic nanoparticles (MNP) coated with 3-aminopropyltriethoxysilane (APTES), Fe(3)O(4)@APTES-RML or RML-M...

Descripción completa

Detalles Bibliográficos
Autores principales: Moreira, Katerine da S., de Oliveira, André L. B., Júnior, Lourembergue S. de M., Monteiro, Rodolpho R. C., da Rocha, Thays N., Menezes, Fernando L., Fechine, Lillian M. U. D., Denardin, Juliano C., Michea, Sebastian, Freire, Rafael M., Fechine, Pierre B. A., Souza, Maria C. M., dos Santos, José C. S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7338345/
https://www.ncbi.nlm.nih.gov/pubmed/32695765
http://dx.doi.org/10.3389/fbioe.2020.00693
_version_ 1783554653044080640
author Moreira, Katerine da S.
de Oliveira, André L. B.
Júnior, Lourembergue S. de M.
Monteiro, Rodolpho R. C.
da Rocha, Thays N.
Menezes, Fernando L.
Fechine, Lillian M. U. D.
Denardin, Juliano C.
Michea, Sebastian
Freire, Rafael M.
Fechine, Pierre B. A.
Souza, Maria C. M.
dos Santos, José C. S.
author_facet Moreira, Katerine da S.
de Oliveira, André L. B.
Júnior, Lourembergue S. de M.
Monteiro, Rodolpho R. C.
da Rocha, Thays N.
Menezes, Fernando L.
Fechine, Lillian M. U. D.
Denardin, Juliano C.
Michea, Sebastian
Freire, Rafael M.
Fechine, Pierre B. A.
Souza, Maria C. M.
dos Santos, José C. S.
author_sort Moreira, Katerine da S.
collection PubMed
description In this communication, it was evaluated the production of fatty acid ethyl ester (FAAE) from the free fatty acids of babassu oil catalyzed by lipase from Rhizomucor miehei (RML) immobilized on magnetic nanoparticles (MNP) coated with 3-aminopropyltriethoxysilane (APTES), Fe(3)O(4)@APTES-RML or RML-MNP for short. MNPs were prepared by co-precipitation coated with 3-aminopropyltriethoxysilane and used as a support to immobilize RML (immobilization yield: 94.7 ± 1.0%; biocatalyst activity: 341.3 ± 1.2 U(p)(–NPB)/g), which were also activated with glutaraldehyde and then used to immobilize RML (immobilization yield: 91.9 ± 0.2%; biocatalyst activity: 199.6 ± 3.5 U(p)(–NPB)/g). RML-MNP was characterized by X-Ray Powder Diffraction (XRPD), Fourier Transform-Infrared (FTIR) spectroscopy and Scanning Electron Microscope (SEM), proving the incorporation and immobilization of RML on the APTES matrix. In addition, the immobilized biocatalyst presented at 60°C a half-life 16–19 times greater than that of the soluble lipase in the pH range 5–10. RML and RML-MNP showed higher activity at pH 7; the immobilized enzyme was more active than the free enzyme in the pH range (5–10) analyzed. For the production of fatty acid ethyl ester, under optimal conditions [40°C, 6 h, 1:1 (FFAs/alcohol)] determined by the Taguchi method, it was possible to obtain conversion of 81.7 ± 0.7% using 5% of RML-MNP.
format Online
Article
Text
id pubmed-7338345
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-73383452020-07-20 Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method Moreira, Katerine da S. de Oliveira, André L. B. Júnior, Lourembergue S. de M. Monteiro, Rodolpho R. C. da Rocha, Thays N. Menezes, Fernando L. Fechine, Lillian M. U. D. Denardin, Juliano C. Michea, Sebastian Freire, Rafael M. Fechine, Pierre B. A. Souza, Maria C. M. dos Santos, José C. S. Front Bioeng Biotechnol Bioengineering and Biotechnology In this communication, it was evaluated the production of fatty acid ethyl ester (FAAE) from the free fatty acids of babassu oil catalyzed by lipase from Rhizomucor miehei (RML) immobilized on magnetic nanoparticles (MNP) coated with 3-aminopropyltriethoxysilane (APTES), Fe(3)O(4)@APTES-RML or RML-MNP for short. MNPs were prepared by co-precipitation coated with 3-aminopropyltriethoxysilane and used as a support to immobilize RML (immobilization yield: 94.7 ± 1.0%; biocatalyst activity: 341.3 ± 1.2 U(p)(–NPB)/g), which were also activated with glutaraldehyde and then used to immobilize RML (immobilization yield: 91.9 ± 0.2%; biocatalyst activity: 199.6 ± 3.5 U(p)(–NPB)/g). RML-MNP was characterized by X-Ray Powder Diffraction (XRPD), Fourier Transform-Infrared (FTIR) spectroscopy and Scanning Electron Microscope (SEM), proving the incorporation and immobilization of RML on the APTES matrix. In addition, the immobilized biocatalyst presented at 60°C a half-life 16–19 times greater than that of the soluble lipase in the pH range 5–10. RML and RML-MNP showed higher activity at pH 7; the immobilized enzyme was more active than the free enzyme in the pH range (5–10) analyzed. For the production of fatty acid ethyl ester, under optimal conditions [40°C, 6 h, 1:1 (FFAs/alcohol)] determined by the Taguchi method, it was possible to obtain conversion of 81.7 ± 0.7% using 5% of RML-MNP. Frontiers Media S.A. 2020-06-30 /pmc/articles/PMC7338345/ /pubmed/32695765 http://dx.doi.org/10.3389/fbioe.2020.00693 Text en Copyright © 2020 Moreira, de Oliveira, Júnior, Monteiro, da Rocha, Menezes, Fechine, Denardin, Michea, Freire, Fechine, Souza and dos Santos. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Moreira, Katerine da S.
de Oliveira, André L. B.
Júnior, Lourembergue S. de M.
Monteiro, Rodolpho R. C.
da Rocha, Thays N.
Menezes, Fernando L.
Fechine, Lillian M. U. D.
Denardin, Juliano C.
Michea, Sebastian
Freire, Rafael M.
Fechine, Pierre B. A.
Souza, Maria C. M.
dos Santos, José C. S.
Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title_full Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title_fullStr Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title_full_unstemmed Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title_short Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method
title_sort lipase from rhizomucor miehei immobilized on magnetic nanoparticles: performance in fatty acid ethyl ester (faee) optimized production by the taguchi method
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7338345/
https://www.ncbi.nlm.nih.gov/pubmed/32695765
http://dx.doi.org/10.3389/fbioe.2020.00693
work_keys_str_mv AT moreirakaterinedas lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT deoliveiraandrelb lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT juniorlouremberguesdem lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT monteirorodolphorc lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT darochathaysn lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT menezesfernandol lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT fechinelillianmud lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT denardinjulianoc lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT micheasebastian lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT freirerafaelm lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT fechinepierreba lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT souzamariacm lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod
AT dossantosjosecs lipasefromrhizomucormieheiimmobilizedonmagneticnanoparticlesperformanceinfattyacidethylesterfaeeoptimizedproductionbythetaguchimethod