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Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions
Immobilization of enzymes is one of the most promising methods in enzyme performance enhancement, including stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still a scientific challenge. Polyethersulfone (PES) and aminated PES (PES–NH...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021891/ https://www.ncbi.nlm.nih.gov/pubmed/24958172 http://dx.doi.org/10.3390/membranes2020198 |
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author | Handayani, Nurrahmi Loos, Katja Wahyuningrum, Deana Buchari, Zulfikar, Muhammad Ali |
author_facet | Handayani, Nurrahmi Loos, Katja Wahyuningrum, Deana Buchari, Zulfikar, Muhammad Ali |
author_sort | Handayani, Nurrahmi |
collection | PubMed |
description | Immobilization of enzymes is one of the most promising methods in enzyme performance enhancement, including stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still a scientific challenge. Polyethersulfone (PES) and aminated PES (PES–NH(2)) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH(2) polymers were successfully fabricated to be applied as bioreactors to increase the immobilized lipase performances. The influence of pore sizes, concentration of additives, and the functional groups that are attached on the PES backbone on enzyme loading and enzyme activity was studied. The largest enzyme loading was obtained by Mucor miehei lipase immobilized onto a PES–NH(2) membrane composed of 10% of PES–NH(2), 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm(2)). Hydrolytic activity of the immobilized lipases indicated that the activities of biocatalysts are not significantly decreased by immobilization. From the reusability test, the lipase immobilized onto PES–NH(2) showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH(2) and PES are 97.16% and 95.37%, respectively), which indicates that this novel material has the potential to be developed as a bioreactor for enzymatic reactions. |
format | Online Article Text |
id | pubmed-4021891 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-40218912014-05-27 Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions Handayani, Nurrahmi Loos, Katja Wahyuningrum, Deana Buchari, Zulfikar, Muhammad Ali Membranes (Basel) Article Immobilization of enzymes is one of the most promising methods in enzyme performance enhancement, including stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still a scientific challenge. Polyethersulfone (PES) and aminated PES (PES–NH(2)) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH(2) polymers were successfully fabricated to be applied as bioreactors to increase the immobilized lipase performances. The influence of pore sizes, concentration of additives, and the functional groups that are attached on the PES backbone on enzyme loading and enzyme activity was studied. The largest enzyme loading was obtained by Mucor miehei lipase immobilized onto a PES–NH(2) membrane composed of 10% of PES–NH(2), 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm(2)). Hydrolytic activity of the immobilized lipases indicated that the activities of biocatalysts are not significantly decreased by immobilization. From the reusability test, the lipase immobilized onto PES–NH(2) showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH(2) and PES are 97.16% and 95.37%, respectively), which indicates that this novel material has the potential to be developed as a bioreactor for enzymatic reactions. MDPI 2012-04-12 /pmc/articles/PMC4021891/ /pubmed/24958172 http://dx.doi.org/10.3390/membranes2020198 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Handayani, Nurrahmi Loos, Katja Wahyuningrum, Deana Buchari, Zulfikar, Muhammad Ali Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title | Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title_full | Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title_fullStr | Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title_full_unstemmed | Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title_short | Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions |
title_sort | immobilization of mucor miehei lipase onto macroporous aminated polyethersulfone membrane for enzymatic reactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4021891/ https://www.ncbi.nlm.nih.gov/pubmed/24958172 http://dx.doi.org/10.3390/membranes2020198 |
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