Next Article in Journal / Special Issue
Seaweed Polysaccharides (Laminarin and Fucoidan) as Functional Ingredients in Pork Meat: An Evaluation of Anti-Oxidative Potential, Thermal Stability and Bioaccessibility
Previous Article in Journal
Synthesis and Bioactivity of Luffarin I
Previous Article in Special Issue
The Potential of Chitosan and Its Derivatives in Prevention and Treatment of Age-Related Diseases
Article Menu

Export Article

Open AccessArticle
Mar. Drugs 2015, 13(4), 2424-2446; doi:10.3390/md13042424

Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization

1
Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, 60965 Poznan, Poland
2
Institute of Inorganic Chemical Technology and Environmental Engineering, West Pomeranian University of Technology, Pulaskiego 10, 70322 Szczecin, Poland
3
Institute of Experimental Physics, TU Bergakademie Freiberg, Leipziger Str. 23, 09599 Freiberg, Germany
4
Adam Mickiewicz University in Poznan, Faculty of Chemistry, Umultowska 89b, 61614 Poznan, Poland
5
Poznan Science and Technology Park, Adam Mickiewicz University Fundation, Rubież 46, 61612 Poznan, Poland
6
Duke University, Center for Materials Genomics, Department of Mechanical Engineering and Materials Science,144 Hudson Hall, Durham, NC 27708, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Paola Laurienzo
Received: 19 February 2015 / Revised: 23 March 2015 / Accepted: 27 March 2015 / Published: 20 April 2015
(This article belongs to the Collection Marine Polysaccharides)
View Full-Text   |   Download PDF [894 KB, uploaded 20 April 2015]   |  

Abstract

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. View Full-Text
Keywords: chitin-lignin matrix; enzyme immobilization; hydrolytic activity; lipase; immobilized lipase stability chitin-lignin matrix; enzyme immobilization; hydrolytic activity; lipase; immobilized lipase stability
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. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Zdarta, J.; Klapiszewski, Ł.; Wysokowski, M.; Norman, M.; Kołodziejczak-Radzimska, A.; Moszyński, D.; Ehrlich, H.; Maciejewski, H.; Stelling, A.L.; Jesionowski, T. Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization. Mar. Drugs 2015, 13, 2424-2446.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top