Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran
Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural in...
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| Format: | Article |
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MDPI AG
2019-10-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/24/20/3648 |
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| author | Zhuofu Wu Linjuan Shi Xiaoxiao Yu Sitong Zhang Guang Chen |
| author_facet | Zhuofu Wu Linjuan Shi Xiaoxiao Yu Sitong Zhang Guang Chen |
| author_sort | Zhuofu Wu |
| collection | DOAJ |
| description | Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes. |
| first_indexed | 2024-12-22T08:25:34Z |
| format | Article |
| id | doaj.art-b23108116abc47049fd6e3787038c90b |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-22T08:25:34Z |
| publishDate | 2019-10-01 |
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| record_format | Article |
| series | Molecules |
| spelling | doaj.art-b23108116abc47049fd6e3787038c90b2022-12-21T18:32:38ZengMDPI AGMolecules1420-30492019-10-012420364810.3390/molecules24203648molecules24203648Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-DiformylfuranZhuofu Wu0Linjuan Shi1Xiaoxiao Yu2Sitong Zhang3Guang Chen4Key Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, ChinaKey Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, ChinaKey Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, ChinaKey Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, ChinaKey Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, ChinaActing as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes.https://www.mdpi.com/1420-3049/24/20/3648co-immobilizationhydroxymethylfurfural2,5-diformylfurangalactose oxidasecatalasehorseradish peroxidase |
| spellingShingle | Zhuofu Wu Linjuan Shi Xiaoxiao Yu Sitong Zhang Guang Chen Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran Molecules co-immobilization hydroxymethylfurfural 2,5-diformylfuran galactose oxidase catalase horseradish peroxidase |
| title | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran |
| title_full | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran |
| title_fullStr | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran |
| title_full_unstemmed | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran |
| title_short | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran |
| title_sort | co immobilization of tri enzymes for the conversion of hydroxymethylfurfural to 2 5 diformylfuran |
| topic | co-immobilization hydroxymethylfurfural 2,5-diformylfuran galactose oxidase catalase horseradish peroxidase |
| url | https://www.mdpi.com/1420-3049/24/20/3648 |
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