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Facile Cellulase Immobilisation on Bioinspired Silica

Cellulases are enzymes with great potential for converting biomass to biofuels for sustainable energy. However, their commercial use is limited by their costs and low reusability. Therefore, the scientific and industrial sectors are focusing on finding better strategies to reuse enzymes and improve...

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Autores principales: Lombardi, Vincenzo, Trande, Matteo, Back, Michele, Patwardhan, Siddharth V., Benedetti, Alvise
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880491/
https://www.ncbi.nlm.nih.gov/pubmed/35214956
http://dx.doi.org/10.3390/nano12040626
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author Lombardi, Vincenzo
Trande, Matteo
Back, Michele
Patwardhan, Siddharth V.
Benedetti, Alvise
author_facet Lombardi, Vincenzo
Trande, Matteo
Back, Michele
Patwardhan, Siddharth V.
Benedetti, Alvise
author_sort Lombardi, Vincenzo
collection PubMed
description Cellulases are enzymes with great potential for converting biomass to biofuels for sustainable energy. However, their commercial use is limited by their costs and low reusability. Therefore, the scientific and industrial sectors are focusing on finding better strategies to reuse enzymes and improve their performance. In this work, cellulase from Aspergillus niger was immobilised through in situ entrapment and adsorption on bio-inspired silica (BIS) supports. To the best of our knowledge, this green effect strategy has never been applied for cellulase into BIS. In situ entrapment was performed during support synthesis, applying a one-pot approach at mild conditions (room temperature, pH 7, and water solvent), while adsorption was performed after support formation. The loading efficiency was investigated on different immobilisation systems by Bradford assay and FTIR. Bovine serum albumin (BSA) was chosen as a control to optimize cellulase loading. The residual activity of cellulase was analysed by the dinitro salicylic acid (DNS) method. Activity of 90% was observed for the entrapped enzyme, while activity of ~55% was observed for the adsorbed enzyme. Moreover, the supported enzyme systems were recycled five times to evaluate their reuse potential. The thermal and pH stability tests suggested that both entrapment and adsorption strategies can increase enzyme activity. The results highlight that the entrapment in BIS is a potentially useful strategy to easily immobilise enzymes, while preserving their stability and recycle potential.
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spelling pubmed-88804912022-02-26 Facile Cellulase Immobilisation on Bioinspired Silica Lombardi, Vincenzo Trande, Matteo Back, Michele Patwardhan, Siddharth V. Benedetti, Alvise Nanomaterials (Basel) Article Cellulases are enzymes with great potential for converting biomass to biofuels for sustainable energy. However, their commercial use is limited by their costs and low reusability. Therefore, the scientific and industrial sectors are focusing on finding better strategies to reuse enzymes and improve their performance. In this work, cellulase from Aspergillus niger was immobilised through in situ entrapment and adsorption on bio-inspired silica (BIS) supports. To the best of our knowledge, this green effect strategy has never been applied for cellulase into BIS. In situ entrapment was performed during support synthesis, applying a one-pot approach at mild conditions (room temperature, pH 7, and water solvent), while adsorption was performed after support formation. The loading efficiency was investigated on different immobilisation systems by Bradford assay and FTIR. Bovine serum albumin (BSA) was chosen as a control to optimize cellulase loading. The residual activity of cellulase was analysed by the dinitro salicylic acid (DNS) method. Activity of 90% was observed for the entrapped enzyme, while activity of ~55% was observed for the adsorbed enzyme. Moreover, the supported enzyme systems were recycled five times to evaluate their reuse potential. The thermal and pH stability tests suggested that both entrapment and adsorption strategies can increase enzyme activity. The results highlight that the entrapment in BIS is a potentially useful strategy to easily immobilise enzymes, while preserving their stability and recycle potential. MDPI 2022-02-13 /pmc/articles/PMC8880491/ /pubmed/35214956 http://dx.doi.org/10.3390/nano12040626 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Lombardi, Vincenzo
Trande, Matteo
Back, Michele
Patwardhan, Siddharth V.
Benedetti, Alvise
Facile Cellulase Immobilisation on Bioinspired Silica
title Facile Cellulase Immobilisation on Bioinspired Silica
title_full Facile Cellulase Immobilisation on Bioinspired Silica
title_fullStr Facile Cellulase Immobilisation on Bioinspired Silica
title_full_unstemmed Facile Cellulase Immobilisation on Bioinspired Silica
title_short Facile Cellulase Immobilisation on Bioinspired Silica
title_sort facile cellulase immobilisation on bioinspired silica
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880491/
https://www.ncbi.nlm.nih.gov/pubmed/35214956
http://dx.doi.org/10.3390/nano12040626
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