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Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties

Commercial cellulase Cellic CTec2 was immobilized by the entrapment technique in sol–gel matrices, and sol–gel entrapment with deposition onto magnetic nanoparticles, using binary or ternary systems of silane precursors with alkyl- or aryl-trimethoxysilanes, at different molar ratios. Appropriate ta...

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Autores principales: Vasilescu, Corina, Marc, Simona, Hulka, Iosif, Paul, Cristina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9602319/
https://www.ncbi.nlm.nih.gov/pubmed/36286127
http://dx.doi.org/10.3390/gels8100626
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author Vasilescu, Corina
Marc, Simona
Hulka, Iosif
Paul, Cristina
author_facet Vasilescu, Corina
Marc, Simona
Hulka, Iosif
Paul, Cristina
author_sort Vasilescu, Corina
collection PubMed
description Commercial cellulase Cellic CTec2 was immobilized by the entrapment technique in sol–gel matrices, and sol–gel entrapment with deposition onto magnetic nanoparticles, using binary or ternary systems of silane precursors with alkyl- or aryl-trimethoxysilanes, at different molar ratios. Appropriate tailoring of the sol–gel matrix allowed for the enhancement of the catalytic efficiency of the cellulase biocatalyst, which was then evaluated in the hydrolysis reaction of Avicel microcrystalline cellulose. A correlation between the catalytic activity with the properties of the sol–gel matrix of the nanobiocatalysts was observed using several characterization methods: scanning electron microscopy (SEM), fluorescence microscopy (FM), Fourier transform infrared spectroscopy (FT-IR) and thermogravimetric analysis (TGA/DTA). The homogeneous distribution of the enzymes in the sol–gel matrix and the mass loss profile as a function of temperature were highlighted. The influence of temperature and pH of the reaction medium on the catalytic performance of the nanobiocatalysts as well as the operational stability under optimized reaction conditions were also investigated; the immobilized biocatalysts proved their superiority in comparison to the native cellulase. The magnetic cellulase biocatalyst with the highest efficiency was reused in seven successive batch hydrolysis cycles of microcrystalline cellulose with remanent activity values that were over 40%, thus we obtained promising results for scaling-up the process.
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spelling pubmed-96023192022-10-27 Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties Vasilescu, Corina Marc, Simona Hulka, Iosif Paul, Cristina Gels Article Commercial cellulase Cellic CTec2 was immobilized by the entrapment technique in sol–gel matrices, and sol–gel entrapment with deposition onto magnetic nanoparticles, using binary or ternary systems of silane precursors with alkyl- or aryl-trimethoxysilanes, at different molar ratios. Appropriate tailoring of the sol–gel matrix allowed for the enhancement of the catalytic efficiency of the cellulase biocatalyst, which was then evaluated in the hydrolysis reaction of Avicel microcrystalline cellulose. A correlation between the catalytic activity with the properties of the sol–gel matrix of the nanobiocatalysts was observed using several characterization methods: scanning electron microscopy (SEM), fluorescence microscopy (FM), Fourier transform infrared spectroscopy (FT-IR) and thermogravimetric analysis (TGA/DTA). The homogeneous distribution of the enzymes in the sol–gel matrix and the mass loss profile as a function of temperature were highlighted. The influence of temperature and pH of the reaction medium on the catalytic performance of the nanobiocatalysts as well as the operational stability under optimized reaction conditions were also investigated; the immobilized biocatalysts proved their superiority in comparison to the native cellulase. The magnetic cellulase biocatalyst with the highest efficiency was reused in seven successive batch hydrolysis cycles of microcrystalline cellulose with remanent activity values that were over 40%, thus we obtained promising results for scaling-up the process. MDPI 2022-10-01 /pmc/articles/PMC9602319/ /pubmed/36286127 http://dx.doi.org/10.3390/gels8100626 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
Vasilescu, Corina
Marc, Simona
Hulka, Iosif
Paul, Cristina
Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title_full Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title_fullStr Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title_full_unstemmed Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title_short Enhancement of the Catalytic Performance and Operational Stability of Sol-Gel-Entrapped Cellulase by Tailoring the Matrix Structure and Properties
title_sort enhancement of the catalytic performance and operational stability of sol-gel-entrapped cellulase by tailoring the matrix structure and properties
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9602319/
https://www.ncbi.nlm.nih.gov/pubmed/36286127
http://dx.doi.org/10.3390/gels8100626
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AT hulkaiosif enhancementofthecatalyticperformanceandoperationalstabilityofsolgelentrappedcellulasebytailoringthematrixstructureandproperties
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