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Tailoring the specificity of the type C feruloyl esterase FoFaeC from Fusarium oxysporum towards methyl sinapate by rational redesign based on small molecule docking simulations
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.ORCID-id: 0000-0002-7754-9398
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.
Department of Chemical Sciences, University of Naples "Federico II".
Department of Chemical Sciences, University of Naples “Federico II”.
Vise andre og tillknytning
2018 (engelsk)Inngår i: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 13, nr 5, artikkel-id e0198127Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The type C feruloyl esterase FoFaeC from Fusarium oxysporum is a newly discovered enzyme with high potential for use in the hydrolysis of lignocellulosic biomass but it shows low activity towards sinapates. In this work, small molecule docking simulations were employed in order to identify important residues for the binding of the four model methyl esters of hydroxycinnamic acids, methyl ferulate/caffeate/sinapate/p-coumarate, to the predicted structure of FoFaeC. Subsequently rational redesign was applied to the enzyme’ active site in order to improve its specificity towards methyl sinapate. A double mutation (F230H/T202V) was considered to provide hydrophobic environment for stabilization of the methoxy substitution on sinapate and a larger binding pocket. Five mutant clones and the wild type were produced in Pichia pastoris and biochemically characterized. All clones showed improved activity, substrate affinity, catalytic efficiency and turnover rate compared to the wild type against methyl sinapate, with clone P13 showing a 5-fold improvement in catalytic efficiency. Although the affinity of all mutant clones was improved against the four model substrates, the catalytic efficiency and turnover rate decreased for the substrates containing a hydroxyl substitution.

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Public Library of Science , 2018. Vol. 13, nr 5, artikkel-id e0198127
HSV kategori
Forskningsprogram
Biokemisk processteknik
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URN: urn:nbn:se:ltu:diva-68904DOI: 10.1371/journal.pone.0198127ISI: 000433084300128PubMedID: 29795702Scopus ID: 2-s2.0-85047458362OAI: oai:DiVA.org:ltu-68904DiVA, id: diva2:1209998
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Validerad;2018;Nivå 2;2018-05-28 (andbra)

Tilgjengelig fra: 2018-05-25 Laget: 2018-05-25 Sist oppdatert: 2019-02-01bibliografisk kontrollert

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Antonopoulou, IoHunt, CameronGerogianni, AlexandraRova, UlrikaChristakopoulos, Paul
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