Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7
β-glucosidases are ubiquitous, well-characterized and biologically important enzymes with considerable uses in industrial sectors. Here, a tetrameric β-glucosidase from Exiguobacterium antarcticum B7 (EaBglA) was immobilized on different activated agarose supports followed by post-immobilization wit...
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ftmdpi:oai:mdpi.com:/2073-4344/9/3/223/ 2023-08-20T04:01:57+02:00 Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 Ricardo Rodrigues de Melo Robson Carlos Alnoch Amanda Silva de Sousa Hélia Harumi Sato Roberto Ruller Cesar Mateo 2019-03-01 application/pdf https://doi.org/10.3390/catal9030223 EN eng Multidisciplinary Digital Publishing Institute Biocatalysis https://dx.doi.org/10.3390/catal9030223 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 9; Issue 3; Pages: 223 β-glucosidase immobilization tetrameric enzyme glutaraldehyde polyethylenimine pH-stability cellobiose hydrolysis Text 2019 ftmdpi https://doi.org/10.3390/catal9030223 2023-07-31T22:04:55Z β-glucosidases are ubiquitous, well-characterized and biologically important enzymes with considerable uses in industrial sectors. Here, a tetrameric β-glucosidase from Exiguobacterium antarcticum B7 (EaBglA) was immobilized on different activated agarose supports followed by post-immobilization with poly-functional macromolecules. The best result was obtained by the immobilization of EaBglA on metal glutaraldehyde-activated agarose support following cross-linking with polyethylenimine. Interestingly, the immobilized EaBglA was 46-fold more stable than its free form and showed optimum pH in the acidic region, with high catalytic activity in the pH range from 3 to 9, while the free EaBglA showed catalytic activity in a narrow pH range (>80% at pH 6.0–8.0) and optimum pH at 7.0. EaBglA had the optimum temperature changed from 30 °C to 50 °C with the immobilization step. The immobilized EaBglA showed an expressive adaptation to pH and it was tolerant to ethanol and glucose, indicating suitable properties involving the saccharification process. Even after 9 cycles of reuse, the immobilized β-glucosidase retained about 100% of its initial activity, demonstrating great operational stability. Hence, the current study describes an efficient strategy to increase the functional characteristics of a tetrameric β-glucosidase for future use in the bioethanol production. Text Antarc* MDPI Open Access Publishing Catalysts 9 3 223 |
institution |
Open Polar |
collection |
MDPI Open Access Publishing |
op_collection_id |
ftmdpi |
language |
English |
topic |
β-glucosidase immobilization tetrameric enzyme glutaraldehyde polyethylenimine pH-stability cellobiose hydrolysis |
spellingShingle |
β-glucosidase immobilization tetrameric enzyme glutaraldehyde polyethylenimine pH-stability cellobiose hydrolysis Ricardo Rodrigues de Melo Robson Carlos Alnoch Amanda Silva de Sousa Hélia Harumi Sato Roberto Ruller Cesar Mateo Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
topic_facet |
β-glucosidase immobilization tetrameric enzyme glutaraldehyde polyethylenimine pH-stability cellobiose hydrolysis |
description |
β-glucosidases are ubiquitous, well-characterized and biologically important enzymes with considerable uses in industrial sectors. Here, a tetrameric β-glucosidase from Exiguobacterium antarcticum B7 (EaBglA) was immobilized on different activated agarose supports followed by post-immobilization with poly-functional macromolecules. The best result was obtained by the immobilization of EaBglA on metal glutaraldehyde-activated agarose support following cross-linking with polyethylenimine. Interestingly, the immobilized EaBglA was 46-fold more stable than its free form and showed optimum pH in the acidic region, with high catalytic activity in the pH range from 3 to 9, while the free EaBglA showed catalytic activity in a narrow pH range (>80% at pH 6.0–8.0) and optimum pH at 7.0. EaBglA had the optimum temperature changed from 30 °C to 50 °C with the immobilization step. The immobilized EaBglA showed an expressive adaptation to pH and it was tolerant to ethanol and glucose, indicating suitable properties involving the saccharification process. Even after 9 cycles of reuse, the immobilized β-glucosidase retained about 100% of its initial activity, demonstrating great operational stability. Hence, the current study describes an efficient strategy to increase the functional characteristics of a tetrameric β-glucosidase for future use in the bioethanol production. |
format |
Text |
author |
Ricardo Rodrigues de Melo Robson Carlos Alnoch Amanda Silva de Sousa Hélia Harumi Sato Roberto Ruller Cesar Mateo |
author_facet |
Ricardo Rodrigues de Melo Robson Carlos Alnoch Amanda Silva de Sousa Hélia Harumi Sato Roberto Ruller Cesar Mateo |
author_sort |
Ricardo Rodrigues de Melo |
title |
Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
title_short |
Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
title_full |
Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
title_fullStr |
Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
title_full_unstemmed |
Cross-Linking with Polyethylenimine Confers Better Functional Characteristics to an Immobilized β-glucosidase from Exiguobacterium antarcticum B7 |
title_sort |
cross-linking with polyethylenimine confers better functional characteristics to an immobilized β-glucosidase from exiguobacterium antarcticum b7 |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
https://doi.org/10.3390/catal9030223 |
genre |
Antarc* |
genre_facet |
Antarc* |
op_source |
Catalysts; Volume 9; Issue 3; Pages: 223 |
op_relation |
Biocatalysis https://dx.doi.org/10.3390/catal9030223 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/catal9030223 |
container_title |
Catalysts |
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9 |
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3 |
container_start_page |
223 |
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1774712332487753728 |