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Understanding the pH-dependent immobilization efficacy of feruloyl esterase-C on mesoporous silica and its structure-activity changes
Chalmers University of Technology, Department of Chemical and Biological Engineering.
Chalmers University of Technology, Department of Chemical and Biological Engineering.
Department of Environmental Science and Technology, Dalian University of Technology.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-0079-5950
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2013 (English)In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, E-ISSN 1873-3158, Vol. 93, p. 65-72Article in journal (Refereed) Published
Abstract [en]

The purpose of the present investigation was to study the pH dependence of both the immobilization process and the enzyme activity of a feruloyl esterase (FoFaeC from Fusarium oxysporum) immobilized in mesoporous silica. This was done by interpreting experimental results with theoretical molecular modeling of the enzyme structure. Modeling of the 3D structure of the enzyme together with calculations of the electrostatic surface potential showed that changes in the electrostatic potential of the protein surface were correlated with the pH dependence of the immobilization process. High immobilization yields were associated with an increase in pH. The transesterification activity of both immobilized and free enzyme was studied at different values of pH and the optimal pH of the immobilized enzyme was found to be one unit lower than that for the free enzyme. The surface charge distribution around the binding pocket was identified as being a crucial factor for the accessibility of the active site of the immobilized enzyme, indicating that the orientation of the enzyme inside the pores is pH dependent. Interestingly, it was observed that the immobilization pH affects the specific activity, irrespective of the changes in reaction pH. This was identified as a pH memory effect for the immobilized enzyme. On the other hand, a change in product selectivity of the immobilized enzyme was also observed when the transesterification reaction was run in MOPS buffer instead of citrate phosphate buffer. Molecular docking studies revealed that the MOPS buffer molecule can bind to the enzyme binding pocket, and can therefore be assumed to modulate the product selectivity of the immobilized enzyme towards transesterification.

Place, publisher, year, edition, pages
2013. Vol. 93, p. 65-72
National Category
Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-9936DOI: 10.1016/j.molcatb.2013.04.011ISI: 000321173300010Scopus ID: 2-s2.0-84878824455Local ID: 8a512d5a-5475-4423-9e3c-8494556baf88OAI: oai:DiVA.org:ltu-9936DiVA, id: diva2:982875
Note
Validerad; 2013; 20130429 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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