Realtime 31P NMR investigation on the catalytic behavior of the enzyme adenylate kinase in the matrix of a switchable ionic liquid

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Per Rogne, Tobias Sparrman, Ikenna Anugwom, Jyri-Pekka Mikkola, Magnus Wolf-Watz
Publication year: 2015
Journal: ChemSusChem
Volume number: 8
Issue number: 22
Start page: 3764
End page: 3768
eISSN: 1864-564X


Abstract

The integration of highly efficient enzymatic catalysis with the solvation properties of ionic liquids for an environmentally friendly and efficient use of raw materials such as wood requires fundamental knowledge about the influence of relevant ionic liquids on enzymes. Switchable ionic liquids (SIL) are promising candidates for implementation of enzymatic treatments of raw materials. One industrially interesting SIL is constituted by monoethanol amine (MEA) and 1,8-diazabicyclo-[5.4.0]-undec-7-ene (DBU) formed with sulfur dioxide (SO2) as the coupling media (DBU-SO2-MEASIL). It has the ability to solubilize the matrix of lignocellulosic biomass while leaving the cellulose backbone intact. Using a novel 31P NMR-based real-time assay we show that this SIL is compatible with enzymatic catalysis because a model enzyme, adenylate kinase, retains its activity in up to at least 25 wt % of DBU-SO2-MEASIL. Thus this SIL appears suitable for, for example, enzymatic degradation of hemicellulose.

Last updated on 2020-23-01 at 03:29