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Optimization of Oligomeric Enzyme Activity in Ionic Liquids Using Rhodotorula Glutinis Yeast Phenylalanine Ammonia Lyase

Optimization of Oligomeric Enzyme Activity in Ionic Liquids Using Rhodotorula Glutinis Yeast Phenylalanine Ammonia Lyase

Christiaan C Barron, Brandon J D Sponagle, Pugazhendhi Arivalagan, Godwin B D'Cunha

Enzyme Microb Technol. 2017 Jan;96:151-156.

PMID: 27871376

Abstract:

Phenylalanine ammonia lyase (E.C.4.3.1.24, PAL) activity of Rhodotorula glutinis yeast has been demonstrated in four commonly used ionic liquids. PAL forward reaction was carried out in 1-butyl-3-methylimidazolium methyl sulfate ([BMIM][MeSO4]), 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF4]), 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]) and 1-butyl-3-methylimidazolium lactate ([BMIM][lactate]). Our experiments have revealed that PAL is catalytically active in ionic liquids and the enzyme activity in ([BMIM][PF6]) is comparable to that obtained in aqueous buffer medium. Different conditions were optimized for maximal PAL forward activity including time of incubation (30.0min)L-phenylalanine substrate concentration (30.0mM), nature of buffer (50.0mM Tris-HCl), pH (9.0), temperature (37°C), and speed of agitation (100 rev min-1). Under these optimized conditions, about 83% conversion of substrate to product was obtained for the PAL forward reaction that was determined using UV spectroscopy at 290nm. PAL reverse reaction in ([BMIM][PF6]) was determined spectrophotometrically at 520nm; and about 59% substrate conversion was obtained. This data provides further knowledge in enzyme biocatalysis in non-aqueous media, and may be of importance when studying the function of other oligomeric/multimeric proteins and enzymes in ionic liquids.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP401788985	1-Butyl-3-methylimidazolium methyl sulfate		401788-98-5	Price

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