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...

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Published in:Journal of Enzymes
Main Authors: Gartner, Patrizia, Rudat, Jens, Bilger, Maximilian, Grünert, Tom, Lanza, Gisela
Other Authors: Ali, Mezni
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
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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
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