Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization
Innovative materials were made via the combination of chitin and lignin, and the immobilization of lipase from Aspergillus niger. Analysis by techniques including FTIR, XPS and 13C CP MAS NMR confirmed the effective immobilization of the enzyme on the surface of the composite support. The electrokin...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-04-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/13/4/2424 |
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| author | Jakub Zdarta Łukasz Klapiszewski Marcin Wysokowski Małgorzata Norman Agnieszka Kołodziejczak-Radzimska Dariusz Moszyński Hermann Ehrlich Hieronim Maciejewski Allison L. Stelling Teofil Jesionowski |
| author_facet | Jakub Zdarta Łukasz Klapiszewski Marcin Wysokowski Małgorzata Norman Agnieszka Kołodziejczak-Radzimska Dariusz Moszyński Hermann Ehrlich Hieronim Maciejewski Allison L. Stelling Teofil Jesionowski |
| author_sort | Jakub Zdarta |
| collection | DOAJ |
| description | Innovative materials were made via the combination of chitin and lignin, and the immobilization of lipase from Aspergillus niger. Analysis by techniques including FTIR, XPS and 13C CP MAS NMR confirmed the effective immobilization of the enzyme on the surface of the composite support. The electrokinetic properties of the resulting systems were also determined. Results obtained from elemental analysis and by the Bradford method enabled the determination of optimum parameters for the immobilization process. Based on the hydrolysis reaction of para-nitrophenyl palmitate, a determination was made of the catalytic activity, thermal and pH stability, and reusability. The systems with immobilized enzymes were found to have a hydrolytic activity of 5.72 mU, and increased thermal and pH stability compared with the native lipase. The products were also shown to retain approximately 80% of their initial catalytic activity, even after 20 reaction cycles. The immobilization process, using a cheap, non-toxic matrix of natural origin, leads to systems with potential applications in wastewater remediation processes and in biosensors. |
| first_indexed | 2024-04-11T14:02:06Z |
| format | Article |
| id | doaj.art-fbdf2098ad7241c8bcf541b9092bf85f |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-11T14:02:06Z |
| publishDate | 2015-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-fbdf2098ad7241c8bcf541b9092bf85f2022-12-22T04:20:06ZengMDPI AGMarine Drugs1660-33972015-04-011342424244610.3390/md13042424md13042424Chitin-Lignin Material as a Novel Matrix for Enzyme ImmobilizationJakub Zdarta0Łukasz Klapiszewski1Marcin Wysokowski2Małgorzata Norman3Agnieszka Kołodziejczak-Radzimska4Dariusz Moszyński5Hermann Ehrlich6Hieronim Maciejewski7Allison L. Stelling8Teofil Jesionowski9Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInstitute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInstitute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInstitute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInstitute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInstitute of Inorganic Chemical Technology and Environmental Engineering, West Pomeranian University of Technology, Pulaskiego 10, 70322 Szczecin, PolandInstitute of Experimental Physics, TU Bergakademie Freiberg, Leipziger Str. 23, 09599 Freiberg, GermanyAdam Mickiewicz University in Poznan, Faculty of Chemistry, Umultowska 89b, 61614 Poznan, PolandDuke University, Center for Materials Genomics, Department of Mechanical Engineering and Materials Science,144 Hudson Hall, Durham, NC 27708, USAInstitute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, PolandInnovative materials were made via the combination of chitin and lignin, and the immobilization of lipase from Aspergillus niger. Analysis by techniques including FTIR, XPS and 13C CP MAS NMR confirmed the effective immobilization of the enzyme on the surface of the composite support. The electrokinetic properties of the resulting systems were also determined. Results obtained from elemental analysis and by the Bradford method enabled the determination of optimum parameters for the immobilization process. Based on the hydrolysis reaction of para-nitrophenyl palmitate, a determination was made of the catalytic activity, thermal and pH stability, and reusability. The systems with immobilized enzymes were found to have a hydrolytic activity of 5.72 mU, and increased thermal and pH stability compared with the native lipase. The products were also shown to retain approximately 80% of their initial catalytic activity, even after 20 reaction cycles. The immobilization process, using a cheap, non-toxic matrix of natural origin, leads to systems with potential applications in wastewater remediation processes and in biosensors.http://www.mdpi.com/1660-3397/13/4/2424chitin-lignin matrixenzyme immobilizationhydrolytic activitylipaseimmobilized lipase stability |
| spellingShingle | Jakub Zdarta Łukasz Klapiszewski Marcin Wysokowski Małgorzata Norman Agnieszka Kołodziejczak-Radzimska Dariusz Moszyński Hermann Ehrlich Hieronim Maciejewski Allison L. Stelling Teofil Jesionowski Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization Marine Drugs chitin-lignin matrix enzyme immobilization hydrolytic activity lipase immobilized lipase stability |
| title | Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization |
| title_full | Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization |
| title_fullStr | Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization |
| title_full_unstemmed | Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization |
| title_short | Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization |
| title_sort | chitin lignin material as a novel matrix for enzyme immobilization |
| topic | chitin-lignin matrix enzyme immobilization hydrolytic activity lipase immobilized lipase stability |
| url | http://www.mdpi.com/1660-3397/13/4/2424 |
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