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Optimization of Transesterification Reactions with CLEA-Immobilized Feruloyl Esterases 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, Wageningen, The Netherlands.
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2018 (English)In: Molecules, ISSN 1420-3049, E-ISSN 1420-3049, Vol. 23, no 9, article id 2403Article in journal (Refereed) Published
Abstract [en]

Feruloyl esterases (FAEs, E.C. 3.1.1.73) are biotechnologically important enzymes with several applications in ferulic acid production from biomass, but also in synthesis of hydroxycinnamic acid derivatives. The use of such biocatalysts in commercial processes can become feasible by their immobilization, providing the advantages of isolation and recycling. In this work, eight feruloyl esterases, immobilized in cross-linked enzyme aggregates (CLEAs) were tested in regard to their transesterification performance, towards the production of prenyl ferulate (PFA) and arabinose ferulate (AFA). After solvent screening, comparison with the activity of respective soluble enzymes, and operational stability tests, FAE125 was selected as the most promising biocatalyst. A central composite design revealed the optimum conditions for each transesterification product, in terms of water content, time, and substrate ratio for both products, and temperature and enzyme load additionally for prenyl ferulate. The optimum product yields obtained were 83.7% for PFA and 58.1% for AFA. FAE125 CLEAs are stable in the optimum conditions of transesterification reactions, maintaining 70% residual activity after five consecutive reactions. Overall, FAE125 CLEAs seem to be able to perform as a robust biocatalyst, offering satisfactory yields and stability, and thus showing significant potential for industrial applications.

Place, publisher, year, edition, pages
MDPI, 2018. Vol. 23, no 9, article id 2403
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Other Industrial Biotechnology Bioprocess Technology
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Biochemical Process Engineering
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URN: urn:nbn:se:ltu:diva-70930DOI: 10.3390/molecules23092403PubMedID: 30235900OAI: oai:DiVA.org:ltu-70930DiVA, id: diva2:1249813
Note

Validerad;2018;Nivå 2;2018-09-25 (svasva)

Available from: 2018-09-20 Created: 2018-09-20 Last updated: 2018-10-10Bibliographically approved

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Zerva, AnastasiaAntonopoulou, IoEnman, JosefineRova, UlrikaChristakopoulos, Paul

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