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Insights into substrate binding of ferulic acid esterases by arabinose and methyl hydroxycinnamate esters and molecular docking
Department of Chemical Engineering, Monash University, Clayton, 3800, Victoria, Australia..
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-7754-9398
Department of Chemical Engineering, Monash University, Clayton, 3800, Victoria, Australia..
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0001-7500-2367
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2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 17315Article in journal (Refereed) Published
Abstract [en]

Ferulic acid esterases (FAE, EC 3.1.1.73) cleave the arabinose hydroxycinnamate ester in plant hemicellulose and other related substrates. FAE are commonly categorised as type A-D based on catalytic activities towards model, short alkyl chain esters of hydroxycinnamates. However, this system correlates poorly with sequence and structural features of the enzymes. In this study, we investigated the basis of the type A categorisation of an FAE from Aspergillus niger, AnFaeA, by comparing its activity toward methyl and arabinose hydroxycinnamate esters. kcat/Km ratios revealed that AnFaeA hydrolysed arabinose ferulate 1600-fold, and arabinose caffeate 6.5 times more efficiently than their methyl ester counterparts. Furthermore, small docking studies showed that while all substrates adopted a catalytic orientation with requisite proximity to the catalytic serine, methyl caffeate and methyl p-coumarate preferentially formed alternative non-catalytic conformations that were energetically favoured. Arabinose ferulate was unable to adopt the alternative conformation while arabinose caffeate preferred the catalytic orientation. This study demonstrates that use of short alkyl chain hydroxycinnnamate esters can result in activity misclassification. The findings of this study provide a basis for developing a robust classification system for FAE and form the basis of sequence-function relationships for this class.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017. Vol. 7, article id 17315
National Category
Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-67020DOI: 10.1038/s41598-017-17260-xISI: 000417570500034PubMedID: 29230049OAI: oai:DiVA.org:ltu-67020DiVA, id: diva2:1166339
Note

Validerad;2018;Nivå 2;2017-12-14 (svasva)

Available from: 2017-12-14 Created: 2017-12-14 Last updated: 2018-05-15Bibliographically approved
In thesis
1. Development of biocatalytic processes for selective antioxidant production
Open this publication in new window or tab >>Development of biocatalytic processes for selective antioxidant production
2018 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Utveckling av biokatalytiska processer för selektivantioxidant produktion
Place, publisher, year, edition, pages
Luleå: Luleå University of Technology, 2018
Series
Doctoral thesis / Luleå University of Technology 1 jan 1997 → …, ISSN 1402-1544
National Category
Other Industrial Biotechnology Chemical Engineering Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
urn:nbn:se:ltu:diva-68343 (URN)978-91-7790-108-2 (ISBN)978-91-7790-109-9 (ISBN)
Public defence
2018-06-12, C305, Luleå, 10:00 (English)
Opponent
Supervisors
Available from: 2018-04-16 Created: 2018-04-13 Last updated: 2018-05-22Bibliographically approved

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