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...
Autores principales: | , , , , , , , , , , , , |
---|---|
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 |