Next Article in Journal
Improved CO-PROX Performance of CuO/CeO2 Catalysts by Using Nanometric Ceria as Support
Next Article in Special Issue
The Synthetic Potential of Fungal Feruloyl Esterases: A Correlation with Current Classification Systems and Predicted Structural Properties
Previous Article in Journal
Fe Oxides Loaded on Carbon Cloth by Hydrothermal Process as an Effective and Reusable Heterogenous Fenton Catalyst
Previous Article in Special Issue
Waste into Fuel—Catalyst and Process Development for MSW Valorisation
Open AccessArticle

Cross-Linked Enzyme Aggregates of Feruloyl Esterase Preparations from Thermothelomyces thermophila and Talaromyces wortmannii

Division of Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, 97187 Luleå, Sweden
DuPont Industrial Biosciences, Nieuwe Kanaal 7-S, 6709 PA Wageningen, The Netherlands
Author to whom correspondence should be addressed.
Catalysts 2018, 8(5), 208;
Received: 18 April 2018 / Revised: 10 May 2018 / Accepted: 10 May 2018 / Published: 15 May 2018
(This article belongs to the Special Issue Novel Enzyme and Whole-Cell Biocatalysis)
PDF [4679 KB, uploaded 15 May 2018]


Cross-linked enzyme aggregates (CLEA®) technology is a well-established method in the current literature for the low-cost and effective immobilization of several enzymes. The main advantage of this particular method is the simplicity of the process, since it consists of only two steps. However, CLEA immobilization must be carefully designed for each desired enzyme, since the optimum conditions for enzymes can vary significantly, according to their physicochemical properties. In the present study, an investigation of the optimum CLEA immobilization conditions was carried out for eight feruloyl esterase preparations. Feruloyl esterases are a very important enzyme group in the valorization of lignocellulosic biomass, since they act in a synergistic way with other enzymes for the breakdown of plant biomass. Specifically, we investigated the type and concentration of precipitant and the crosslinker concentration, for retaining optimal activity. FAE68 was found to be the most promising enzyme for CLEA immobilization, since in this case, the maximum retained activity, over 98%, was observed. Subsequently, we examined the operational stability and the stability in organic solvents for the obtained CLEA preparations, as well as their structure. Overall, our results support that the maximum activity retaining and the stability properties of the final CLEAs can vary greatly in different FAE preparations. Nevertheless, some of the examined FAEs show a significant potential for further applications in harsh industrial conditions. View Full-Text
Keywords: cross-linked enzyme aggregates; feruloyl esterases; ferulic acid; enzyme immobilization cross-linked enzyme aggregates; feruloyl esterases; ferulic acid; enzyme immobilization

Figure 1

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).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Zerva, A.; Antonopoulou, I.; Enman, J.; Iancu, L.; Rova, U.; Christakopoulos, P. Cross-Linked Enzyme Aggregates of Feruloyl Esterase Preparations from Thermothelomyces thermophila and Talaromyces wortmannii. Catalysts 2018, 8, 208.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Catalysts EISSN 2073-4344 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top