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Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid
Cellulase from Aspergillus niger was immobilized onto β-cyclodextrin-conjugated magnetic particles by silanization and reductive amidation. The immobilized cellulase gained supermagnetism due to the magnetic nanoparticles. Ninety percent of cellulase was immobilized, but the activity of immobilized...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385602/ https://www.ncbi.nlm.nih.gov/pubmed/25874210 http://dx.doi.org/10.1155/2015/409103 |
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author | Huang, Po-Jung Chang, Ken-Lin Hsieh, Jung-Feng Chen, Shui-Tein |
author_facet | Huang, Po-Jung Chang, Ken-Lin Hsieh, Jung-Feng Chen, Shui-Tein |
author_sort | Huang, Po-Jung |
collection | PubMed |
description | Cellulase from Aspergillus niger was immobilized onto β-cyclodextrin-conjugated magnetic particles by silanization and reductive amidation. The immobilized cellulase gained supermagnetism due to the magnetic nanoparticles. Ninety percent of cellulase was immobilized, but the activity of immobilized cellulase decreased by 10%. In this study, ionic liquid (1-butyl-3-methylimidazolium chloride) was introduced into the hydrolytic process because the original reaction was a solid-solid reaction. The activity of immobilized cellulase was improved from 54.87 to 59.11 U g immobilized cellulase(−1) at an ionic liquid concentration of 200 mM. Using immobilized cellulase and ionic liquid in the hydrolysis of rice straw, the initial reaction rate was increased from 1.629 to 2.739 g h(−1) L(−1). One of the advantages of immobilized cellulase is high reusability—it was usable for a total of 16 times in this study. Compared with free cellulase, magnetized cellulase can be recycled by magnetic field and the activity of immobilized cellulase was shown to remain at 85% of free cellulase without denaturation under a high concentration of glucose (15 g L(−1)). Therefore, immobilized cellulase can hydrolyze rice straw continuously compared with free cellulase. The amount of harvested glucose can be up to twentyfold higher than that from the hydrolysis by free cellulase. |
format | Online Article Text |
id | pubmed-4385602 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-43856022015-04-13 Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid Huang, Po-Jung Chang, Ken-Lin Hsieh, Jung-Feng Chen, Shui-Tein Biomed Res Int Research Article Cellulase from Aspergillus niger was immobilized onto β-cyclodextrin-conjugated magnetic particles by silanization and reductive amidation. The immobilized cellulase gained supermagnetism due to the magnetic nanoparticles. Ninety percent of cellulase was immobilized, but the activity of immobilized cellulase decreased by 10%. In this study, ionic liquid (1-butyl-3-methylimidazolium chloride) was introduced into the hydrolytic process because the original reaction was a solid-solid reaction. The activity of immobilized cellulase was improved from 54.87 to 59.11 U g immobilized cellulase(−1) at an ionic liquid concentration of 200 mM. Using immobilized cellulase and ionic liquid in the hydrolysis of rice straw, the initial reaction rate was increased from 1.629 to 2.739 g h(−1) L(−1). One of the advantages of immobilized cellulase is high reusability—it was usable for a total of 16 times in this study. Compared with free cellulase, magnetized cellulase can be recycled by magnetic field and the activity of immobilized cellulase was shown to remain at 85% of free cellulase without denaturation under a high concentration of glucose (15 g L(−1)). Therefore, immobilized cellulase can hydrolyze rice straw continuously compared with free cellulase. The amount of harvested glucose can be up to twentyfold higher than that from the hydrolysis by free cellulase. Hindawi Publishing Corporation 2015 2015-03-22 /pmc/articles/PMC4385602/ /pubmed/25874210 http://dx.doi.org/10.1155/2015/409103 Text en Copyright © 2015 Po-Jung Huang et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Huang, Po-Jung Chang, Ken-Lin Hsieh, Jung-Feng Chen, Shui-Tein Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title | Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title_full | Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title_fullStr | Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title_full_unstemmed | Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title_short | Catalysis of Rice Straw Hydrolysis by the Combination of Immobilized Cellulase from Aspergillus niger on β-Cyclodextrin-Fe(3)O(4) Nanoparticles and Ionic Liquid |
title_sort | catalysis of rice straw hydrolysis by the combination of immobilized cellulase from aspergillus niger on β-cyclodextrin-fe(3)o(4) nanoparticles and ionic liquid |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385602/ https://www.ncbi.nlm.nih.gov/pubmed/25874210 http://dx.doi.org/10.1155/2015/409103 |
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