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Realtime 31 P NMR Investigation on the Catalytic Behavior of the Enzyme Adenylate kinase in the Matrix of a Switchable Ionic Liquid
Author(s) -
Rogne Per,
Sparrman Tobias,
Anugwom Ikenna,
Mikkola JyriPekka,
WolfWatz Magnus
Publication year - 2015
Publication title -
chemsuschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.412
H-Index - 157
eISSN - 1864-564X
pISSN - 1864-5631
DOI - 10.1002/cssc.201501104
Subject(s) - ionic liquid , chemistry , catalysis , cellulose , enzyme catalysis , organic chemistry , biocatalysis , amination , combinatorial chemistry , green chemistry
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 (SO 2 ) as the coupling media (DBU‐SO 2 ‐MEASIL). It has the ability to solubilize the matrix of lignocellulosic biomass while leaving the cellulose backbone intact. Using a novel 31 P 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‐SO 2 ‐MEASIL. Thus this SIL appears suitable for, for example, enzymatic degradation of hemicellulose.