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Real-time 31P NMR investigation on the catalytic behavior of the enzyme Adenylate kinase in the matrix of a switchable ionic liquid
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- Rogne, Per (author)
- Umeå universitet,Kemiska institutionen
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- Sparrman, Tobias, 1970- (author)
- Umeå universitet,Kemiska institutionen
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- Anugwom, Ikenna (author)
- Umeå universitet,Kemiska institutionen
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- (creator_code:org_t)
- 2015-10-23
- 2015
- English.
- In: ChemSusChem. - : John Wiley & Sons. - 1864-5631 .- 1864-564X. ; 8:2, s. 3764-3768
- Journal article (peer-reviewed)
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Keyword
- cellulose
- enzymes
- green chemistry
- NMR spectroscopy
- ionic liquids
Publication and Content Type
- ref (subject category)
- art (subject category)
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