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Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound

We have developed an integrated, multienzyme functionalized membrane reactor for bioconversion of a lignin model compound involving enzymatic catalysis. The membrane bioreactors were fabricated through the layer-by-layer assembly approach to immobilize three different enzymes (glucose oxidase, perox...

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Autores principales: Sarma, Rupam, Islam, Md. Saiful, Running, Mark P., Bhattacharyya, Dibakar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6358281/
https://www.ncbi.nlm.nih.gov/pubmed/30719335
http://dx.doi.org/10.3390/polym10040463
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author Sarma, Rupam
Islam, Md. Saiful
Running, Mark P.
Bhattacharyya, Dibakar
author_facet Sarma, Rupam
Islam, Md. Saiful
Running, Mark P.
Bhattacharyya, Dibakar
author_sort Sarma, Rupam
collection PubMed
description We have developed an integrated, multienzyme functionalized membrane reactor for bioconversion of a lignin model compound involving enzymatic catalysis. The membrane bioreactors were fabricated through the layer-by-layer assembly approach to immobilize three different enzymes (glucose oxidase, peroxidase and laccase) into pH-responsive membranes. This novel membrane reactor couples the in situ generation of hydrogen peroxide (by glucose oxidase) to oxidative conversion of a lignin model compound, guaiacylglycerol-β-guaiacyl ether (GGE). Preliminary investigation of the efficacy of these functional membranes towards GGE degradation is demonstrated under convective flow mode. Over 90% of the initial feed could be degraded with the multienzyme immobilized membranes at a residence time of approximately 22 s. GGE conversion product analysis revealed the formation of oligomeric oxidation products upon reaction with peroxidase, which may be a potential hazard to membrane bioreactors. These oxidation products could further be degraded by laccase enzymes in the multienzymatic membranes, explaining the potential of multi enzyme membrane reactors. The multienzyme incorporated membrane reactors were active for more than 30 days of storage time at 4 °C. During this time span, repetitive use of the membrane reactor was demonstrated involving 5–6 h of operation time for each cycle. The membrane reactor displayed encouraging performance, losing only 12% of its initial activity after multiple cycles of operation.
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spelling pubmed-63582812019-04-01 Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound Sarma, Rupam Islam, Md. Saiful Running, Mark P. Bhattacharyya, Dibakar Polymers (Basel) Article We have developed an integrated, multienzyme functionalized membrane reactor for bioconversion of a lignin model compound involving enzymatic catalysis. The membrane bioreactors were fabricated through the layer-by-layer assembly approach to immobilize three different enzymes (glucose oxidase, peroxidase and laccase) into pH-responsive membranes. This novel membrane reactor couples the in situ generation of hydrogen peroxide (by glucose oxidase) to oxidative conversion of a lignin model compound, guaiacylglycerol-β-guaiacyl ether (GGE). Preliminary investigation of the efficacy of these functional membranes towards GGE degradation is demonstrated under convective flow mode. Over 90% of the initial feed could be degraded with the multienzyme immobilized membranes at a residence time of approximately 22 s. GGE conversion product analysis revealed the formation of oligomeric oxidation products upon reaction with peroxidase, which may be a potential hazard to membrane bioreactors. These oxidation products could further be degraded by laccase enzymes in the multienzymatic membranes, explaining the potential of multi enzyme membrane reactors. The multienzyme incorporated membrane reactors were active for more than 30 days of storage time at 4 °C. During this time span, repetitive use of the membrane reactor was demonstrated involving 5–6 h of operation time for each cycle. The membrane reactor displayed encouraging performance, losing only 12% of its initial activity after multiple cycles of operation. MDPI 2018-04-23 /pmc/articles/PMC6358281/ /pubmed/30719335 http://dx.doi.org/10.3390/polym10040463 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sarma, Rupam
Islam, Md. Saiful
Running, Mark P.
Bhattacharyya, Dibakar
Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title_full Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title_fullStr Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title_full_unstemmed Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title_short Multienzyme Immobilized Polymeric Membrane Reactor for the Transformation of a Lignin Model Compound
title_sort multienzyme immobilized polymeric membrane reactor for the transformation of a lignin model compound
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6358281/
https://www.ncbi.nlm.nih.gov/pubmed/30719335
http://dx.doi.org/10.3390/polym10040463
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