Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization
Jakub Zdarta,
Łukasz Klapiszewski,
Marcin Wysokowski,
Małgorzata Norman,
Agnieszka Kołodziejczak-Radzimska,
Dariusz Moszyński,
Hermann Ehrlich,
Hieronim Maciejewski,
Allison L. Stelling,
Teofil Jesionowski
Affiliations
Jakub Zdarta
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
Łukasz Klapiszewski
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
Marcin Wysokowski
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
Małgorzata Norman
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
Agnieszka Kołodziejczak-Radzimska
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
Dariusz Moszyński
Institute of Inorganic Chemical Technology and Environmental Engineering, West Pomeranian University of Technology, Pulaskiego 10, 70322 Szczecin, Poland
Hermann Ehrlich
Institute of Experimental Physics, TU Bergakademie Freiberg, Leipziger Str. 23, 09599 Freiberg, Germany
Hieronim Maciejewski
Adam Mickiewicz University in Poznan, Faculty of Chemistry, Umultowska 89b, 61614 Poznan, Poland
Allison L. Stelling
Duke University, Center for Materials Genomics, Department of Mechanical Engineering and Materials Science,144 Hudson Hall, Durham, NC 27708, USA
Teofil Jesionowski
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
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.
