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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2012-04-01
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| Series: | Membranes |
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| Online Access: | http://www.mdpi.com/2077-0375/2/2/198/ |
| _version_ | 1797707468537593856 |
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| author | Deana Wahyuningrum Nurrahmi Handayani Buchari Muhammad Ali Zulfikar Katja Loos |
| author_facet | Deana Wahyuningrum Nurrahmi Handayani Buchari Muhammad Ali Zulfikar Katja Loos |
| author_sort | Deana Wahyuningrum |
| collection | DOAJ |
| 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–NH2) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH2 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–NH2 membrane composed of 10% of PES–NH2, 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm2). 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–NH2 showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH2 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. |
| first_indexed | 2024-03-12T06:07:49Z |
| format | Article |
| id | doaj.art-8664d77e0fe44f8084e8a07d94c2c02d |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-12T06:07:49Z |
| publishDate | 2012-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-8664d77e0fe44f8084e8a07d94c2c02d2023-09-03T03:28:08ZengMDPI AGMembranes2077-03752012-04-012219821310.3390/membranes2020198Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic ReactionsDeana WahyuningrumNurrahmi HandayaniBuchariMuhammad Ali ZulfikarKatja LoosImmobilization 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–NH2) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH2 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–NH2 membrane composed of 10% of PES–NH2, 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm2). 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–NH2 showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH2 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.http://www.mdpi.com/2077-0375/2/2/198/aminated PESsolid supportMucor mieheienzymatic reactionslipase immobilization |
| spellingShingle | Deana Wahyuningrum Nurrahmi Handayani Buchari Muhammad Ali Zulfikar Katja Loos Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions Membranes aminated PES solid support Mucor miehei enzymatic reactions lipase immobilization |
| 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 | aminated PES solid support Mucor miehei enzymatic reactions lipase immobilization |
| url | http://www.mdpi.com/2077-0375/2/2/198/ |
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