Next Article in Journal
Retraction: Beltaïef et al. An Expeditious Synthesis of [1,2]Isoxazolidin-5-ones and [1,2]Oxazin-6-ones from Functional Allyl Bromide Derivatives. Molecules 2010, 15, 4094-4101
Next Article in Special Issue
Enzymatic Cellulose Hydrolysis: Enzyme Reusability and Visualization of β-Glucosidase Immobilized in Calcium Alginate
Previous Article in Journal
Biomimetic Adhesive Materials Containing Cyanoacryl Group for Medical Application
Previous Article in Special Issue
Immobilization of Horseradish Peroxidase on NH2-Modified Magnetic Fe3O4/SiO2 Particles and Its Application in Removal of 2,4-Dichlorophenol
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Molecules 2014, 19(10), 16794-16809; doi:10.3390/molecules191016794

Substrate Specificity and Enzyme Recycling Using Chitosan Immobilized Laccase

1
Laboratório de Tratamento de Águas e Efluentes, Departamento de Engenharia Ambiental, Universidade do Estado de Santa Catarina, Lages 88520-000, Brazil
2
Laboratório de Engenharia Bioquímica, Departamento de Engenharia Química e Engenharia de Alimentos, Universidade Federal de Santa Catarina, Florianópolis 88040-900, Brazil
3
Laboratório de Bioquímica, Departamento de Produção Animal e Alimentos, Universidade do Estado de Santa Catarina, Lages 88520-000, Brazil
4
Grupo de Catálise Enzimática e Síntese Orgânica, Departamento de Engenharia Química, Universidade do Sul de Santa Catarina, Tubarão 88704-900, Brazil
5
Laboratório de Avaliação Exotoxicológica, Departamento de Bioquímica, Universidade Federal de Santa Catarina, Florianópolis 88040-900, Brazil
*
Author to whom correspondence should be addressed.
Received: 16 May 2014 / Revised: 22 September 2014 / Accepted: 8 October 2014 / Published: 17 October 2014
(This article belongs to the Special Issue Enzyme Immobilization)
View Full-Text   |   Download PDF [389 KB, uploaded 17 October 2014]   |  

Abstract

The immobilization of laccase (Aspergillus sp.) on chitosan by cross-linking and its application in bioconversion of phenolic compounds in batch reactors were studied. Investigation was performed using laccase immobilized via chemical cross-linking due to the higher enzymatic operational stability of this method as compared to immobilization via physical adsorption. To assess the influence of different substrate functional groups on the enzyme’s catalytic efficiency, substrate specificity was investigated using chitosan-immobilized laccase and eighteen different phenol derivatives. It was observed that 4-nitrophenol was not oxidized, while 2,5-xylenol, 2,6-xylenol, 2,3,5-trimethylphenol, syringaldazine, 2,6-dimetoxyphenol and ethylphenol showed reaction yields up 90% at 40 °C. The kinetic of process, enzyme recyclability and operational stability were studied. In batch reactors, it was not possible to reuse the enzyme when it was applied to syringaldazne bioconversion. However, when the enzyme was applied to bioconversion of 2,6-DMP, the activity was stable for eight reaction batches. View Full-Text
Keywords: laccase; Aspergillus sp.; chitosan; enzyme immobilization; phenolic compounds; bioremediation laccase; Aspergillus sp.; chitosan; enzyme immobilization; phenolic compounds; bioremediation
Figures

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

Skoronski, E.; Fernandes, M.; Magalhães, M.L.B.; da Silva, G.F.; João, J.J.; Soares, C.H.L.; Júnior, A.F. Substrate Specificity and Enzyme Recycling Using Chitosan Immobilized Laccase. Molecules 2014, 19, 16794-16809.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top