Real-time 31P NMR investigation on the catalytic behavior of the enzyme Adenylate kinase in the matrix of a switchable ionic liquidVisa övriga samt affilieringar
2015 (Engelska)Ingår i: ChemSusChem, ISSN 1864-5631, E-ISSN 1864-564X, Vol. 8, nr 2, s. 3764-3768Artikel i tidskrift (Refereegranskat) Published
Abstract [en]
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.
Ort, förlag, år, upplaga, sidor
John Wiley & Sons, 2015. Vol. 8, nr 2, s. 3764-3768
Nyckelord [en]
cellulose, enzymes, green chemistry, NMR spectroscopy, ionic liquids
Nationell ämneskategori
Kemi
Identifikatorer
URN: urn:nbn:se:umu:diva-110689DOI: 10.1002/cssc.201501104ISI: 000365752200003Scopus ID: 2-s2.0-84948162355OAI: oai:DiVA.org:umu-110689DiVA, id: diva2:864247
2015-10-262015-10-262023-03-23Bibliografiskt granskad