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Cross-Linked Enzyme Aggregates of Feruloyl Esterase Preparations from Thermothelomyces thermophila and Talaromyces wortmannii
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0003-0361-7690
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-7754-9398
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-6337-6924
DuPont Industrial Biosciences, Nieuwe Kanaal 7-S, 6709 PA Wageningen, The Netherlands.
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2018 (English)In: Catalysts, ISSN 2073-4344, Vol. 8, no 5, article id 208Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
MDPI , 2018. Vol. 8, no 5, article id 208
National Category
Chemical Engineering Bioprocess Technology
Research subject
Biochemical Process Engineering
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URN: urn:nbn:se:ltu:diva-68931DOI: 10.3390/catal8050208ISI: 000435191500037Scopus ID: 2-s2.0-85048056816OAI: oai:DiVA.org:ltu-68931DiVA, id: diva2:1210277
Note

Validerad;2018;Nivå 2;2018-06-05 (rokbeg)

Available from: 2018-05-28 Created: 2018-05-28 Last updated: 2018-06-28Bibliographically approved

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Publisher's full textScopushttp://www.mdpi.com/2073-4344/8/5/208

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Zerva, AnastasiaAntonopoulou, IoEnman, JosefineRova, UlrikaChristakopoulos, Paul

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