Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles
Magnetic Fe3O4 nanoparticles were successfully functionalized with the low-cost mussel-inspired tannic acid (TA)/polyethylenimine (PEI) under mild conditions and then activated with glutaraldehyde (GA) to covalently immobilize laccase for degradation of four model phenolic inhibitors commonly found...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-09-01
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| Series: | Results in Engineering |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590123022002559 |
| _version_ | 1818479597164953600 |
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| author | Shiqian Li Benkun Qi Jianquan Luo Yinhua Wan |
| author_facet | Shiqian Li Benkun Qi Jianquan Luo Yinhua Wan |
| author_sort | Shiqian Li |
| collection | DOAJ |
| description | Magnetic Fe3O4 nanoparticles were successfully functionalized with the low-cost mussel-inspired tannic acid (TA)/polyethylenimine (PEI) under mild conditions and then activated with glutaraldehyde (GA) to covalently immobilize laccase for degradation of four model phenolic inhibitors commonly found in lignocellulosic hydrolysate. The immobilized laccase showed the highest relative enzyme activity with the laccase loading of 39.9 mg/g and the enzyme activity recovery of 53.1%. Compared with free laccase, immobilized laccase possessed better relative enzyme activity at acidic pH and wide temperature range, as well as exhibited excellent storage stability and satisfactory reusability. Moreover, it was found that the phenolic degradation products by immobilized laccase did not exhibit obvious inhibition on subsequent enzymatic cellulose hydrolysis. Thus, the low-cost TA/PEI coating for modification of magnetic nanoparticles will provide a promising support for laccase immobilization and the immobilized laccase has great potential in removal of phenolic inhibitors present in lignocellulosic hydrolysate. |
| first_indexed | 2024-12-10T11:12:52Z |
| format | Article |
| id | doaj.art-67a1b430acac4e4986e94eb7181d7557 |
| institution | Directory Open Access Journal |
| issn | 2590-1230 |
| language | English |
| last_indexed | 2024-12-10T11:12:52Z |
| publishDate | 2022-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Results in Engineering |
| spelling | doaj.art-67a1b430acac4e4986e94eb7181d75572022-12-22T01:51:20ZengElsevierResults in Engineering2590-12302022-09-0115100585Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticlesShiqian Li0Benkun Qi1Jianquan Luo2Yinhua Wan3State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; University of Chinese Academy of Sciences, Beijing, 100049, PR ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Corresponding author.State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; University of Chinese Academy of Sciences, Beijing, 100049, PR ChinaUniversity of Chinese Academy of Sciences, Beijing, 100049, PR China; Ganjiang Innovation Academy, Chinese Academy of Sciences, Ganzhou, Jiangxi, PR ChinaMagnetic Fe3O4 nanoparticles were successfully functionalized with the low-cost mussel-inspired tannic acid (TA)/polyethylenimine (PEI) under mild conditions and then activated with glutaraldehyde (GA) to covalently immobilize laccase for degradation of four model phenolic inhibitors commonly found in lignocellulosic hydrolysate. The immobilized laccase showed the highest relative enzyme activity with the laccase loading of 39.9 mg/g and the enzyme activity recovery of 53.1%. Compared with free laccase, immobilized laccase possessed better relative enzyme activity at acidic pH and wide temperature range, as well as exhibited excellent storage stability and satisfactory reusability. Moreover, it was found that the phenolic degradation products by immobilized laccase did not exhibit obvious inhibition on subsequent enzymatic cellulose hydrolysis. Thus, the low-cost TA/PEI coating for modification of magnetic nanoparticles will provide a promising support for laccase immobilization and the immobilized laccase has great potential in removal of phenolic inhibitors present in lignocellulosic hydrolysate.http://www.sciencedirect.com/science/article/pii/S2590123022002559Magnetic nanoparticlesEnzyme immobilizationLaccaseCatechol/polyamineTannic acid |
| spellingShingle | Shiqian Li Benkun Qi Jianquan Luo Yinhua Wan Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles Results in Engineering Magnetic nanoparticles Enzyme immobilization Laccase Catechol/polyamine Tannic acid |
| title | Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles |
| title_full | Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles |
| title_fullStr | Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles |
| title_full_unstemmed | Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles |
| title_short | Degradation of phenolic inhibitors by laccase immobilized on tannic acid/polyethylenimine modified magnetic nanoparticles |
| title_sort | degradation of phenolic inhibitors by laccase immobilized on tannic acid polyethylenimine modified magnetic nanoparticles |
| topic | Magnetic nanoparticles Enzyme immobilization Laccase Catechol/polyamine Tannic acid |
| url | http://www.sciencedirect.com/science/article/pii/S2590123022002559 |
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