Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes?
Polymer electrolyte membrane (PEM) technologies hold promise for sustainable energy solutions, yet pinhole-related challenges persist. Our research introduces a novel biohybrid approach to self-healing, enhancing multiple healing cycles with minimal membrane disruption. Initial steps involve immobil...
Published in: | Journal of Enzymes |
---|---|
Main Authors: | , , , , |
Other Authors: | |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Open Access Pub
2023
|
Subjects: | |
Online Access: | http://dx.doi.org/10.14302/issn.2690-4829.jen-23-4799 https://openaccesspub.org/jen/article/2036 |
id |
cropenaccpub:10.14302/issn.2690-4829.jen-23-4799 |
---|---|
record_format |
openpolar |
spelling |
cropenaccpub:10.14302/issn.2690-4829.jen-23-4799 2024-05-19T07:32:18+00:00 Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? Gartner, Patrizia Rudat, Jens Bilger, Maximilian Grünert, Tom Lanza, Gisela Ali, Mezni 2023 http://dx.doi.org/10.14302/issn.2690-4829.jen-23-4799 https://openaccesspub.org/jen/article/2036 en eng Open Access Pub Journal of Enzymes volume 1, issue 3, page 1-12 ISSN 2690-4829 journal-article 2023 cropenaccpub https://doi.org/10.14302/issn.2690-4829.jen-23-4799 2024-05-01T06:52:25Z Polymer electrolyte membrane (PEM) technologies hold promise for sustainable energy solutions, yet pinhole-related challenges persist. Our research introduces a novel biohybrid approach to self-healing, enhancing multiple healing cycles with minimal membrane disruption. Initial steps involve immobilizing enzymes on a polymeric membrane. This study establishes the immobilization process and analytical framework through enzyme immobilization on polypropylene. Applicability and stability are investigated, laying groundwork for potential Nafion™ applications and advancing climate neutral energy. Qualitative analysis employs colorimetric p-NPA assay on polypropylene-immobilized lipase from Candida rugosa (CRL) and Lipase B from Candida antarctica (CALB). Both enzymes hold their temperature optimum at 50°C which is increased by 10°C via immobilization. Diisopropylcarbodiimide (DIC) is optimal for immobilization. Synchronous enzyme and DIC addition is advantageous. After 8 reuse cycles, immobilized enzymes retain 54.3% residual activity. Immobilizates exposed to PEM fuel cell conditions show better stability due to covalent immobilization than free CRL. Yet, declines occur under stressors like 60 °C and concentrated alcohol. Immobilizates remain resilient at pH 3 and under oxidizing as well as reducing conditions constituted by varied gas atmospheres. Considering PEM fuel cells' operational range, in-depth investigations across conditions are vital. Future studies target long-term PEM fuel cell lifespans, focusing on extremophilic enzymes or modifications for high-temperature stability. Subsequently, the transferability of the immobilization method to Nafion™ shall be deliberated based on the outcomes. Article in Journal/Newspaper Antarc* Antarctica Open Access Pub (OAP) Journal of Enzymes 1 3 1 12 |
institution |
Open Polar |
collection |
Open Access Pub (OAP) |
op_collection_id |
cropenaccpub |
language |
English |
description |
Polymer electrolyte membrane (PEM) technologies hold promise for sustainable energy solutions, yet pinhole-related challenges persist. Our research introduces a novel biohybrid approach to self-healing, enhancing multiple healing cycles with minimal membrane disruption. Initial steps involve immobilizing enzymes on a polymeric membrane. This study establishes the immobilization process and analytical framework through enzyme immobilization on polypropylene. Applicability and stability are investigated, laying groundwork for potential Nafion™ applications and advancing climate neutral energy. Qualitative analysis employs colorimetric p-NPA assay on polypropylene-immobilized lipase from Candida rugosa (CRL) and Lipase B from Candida antarctica (CALB). Both enzymes hold their temperature optimum at 50°C which is increased by 10°C via immobilization. Diisopropylcarbodiimide (DIC) is optimal for immobilization. Synchronous enzyme and DIC addition is advantageous. After 8 reuse cycles, immobilized enzymes retain 54.3% residual activity. Immobilizates exposed to PEM fuel cell conditions show better stability due to covalent immobilization than free CRL. Yet, declines occur under stressors like 60 °C and concentrated alcohol. Immobilizates remain resilient at pH 3 and under oxidizing as well as reducing conditions constituted by varied gas atmospheres. Considering PEM fuel cells' operational range, in-depth investigations across conditions are vital. Future studies target long-term PEM fuel cell lifespans, focusing on extremophilic enzymes or modifications for high-temperature stability. Subsequently, the transferability of the immobilization method to Nafion™ shall be deliberated based on the outcomes. |
author2 |
Ali, Mezni |
format |
Article in Journal/Newspaper |
author |
Gartner, Patrizia Rudat, Jens Bilger, Maximilian Grünert, Tom Lanza, Gisela |
spellingShingle |
Gartner, Patrizia Rudat, Jens Bilger, Maximilian Grünert, Tom Lanza, Gisela Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
author_facet |
Gartner, Patrizia Rudat, Jens Bilger, Maximilian Grünert, Tom Lanza, Gisela |
author_sort |
Gartner, Patrizia |
title |
Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
title_short |
Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
title_full |
Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
title_fullStr |
Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
title_full_unstemmed |
Enzyme Immobilization On Polypropylene Film: A Role Model For Biocatalytic Polymer Membranes? |
title_sort |
enzyme immobilization on polypropylene film: a role model for biocatalytic polymer membranes? |
publisher |
Open Access Pub |
publishDate |
2023 |
url |
http://dx.doi.org/10.14302/issn.2690-4829.jen-23-4799 https://openaccesspub.org/jen/article/2036 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Journal of Enzymes volume 1, issue 3, page 1-12 ISSN 2690-4829 |
op_doi |
https://doi.org/10.14302/issn.2690-4829.jen-23-4799 |
container_title |
Journal of Enzymes |
container_volume |
1 |
container_issue |
3 |
container_start_page |
1 |
op_container_end_page |
12 |
_version_ |
1799470296583897088 |