Optimization of oligomeric enzyme activity in ionic liquids using Rhodotorula glutinis yeast phenylalanine ammonia lyase
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- 作者：Christiaan C. Barron ; Pharmacy Candidatea ; Brandon J.D. Sponagleb ; Pugazhendhi Arivalaganc ; Godwin B. D&rsquo ; Cunha ; PhDb ; godwin_dcunha@cbu.ca" class="auth_mail" title="E-mail the corresponding author (Associate Professor)
- 关键词：PAL ; phenylalanine ammonia lyase ; [BMIM][MeSO4] ; 1-butyl-3-methylimidazolium methyl sulfate ; [BMIM][BF4] ; 1-butyl-3-methylimidazolium tetrafluoroborate ; [BMIM][PF6] ; 1-butyl-3-methylimidazolium hexafluorophosphate ; [BMIM][lactate] ; 1-butyl-3-methylimidazolium lactate ; OS ; organic solvents ; ILs ; ionic liquids ; L-Phe ; L-phenylalanine ; t-CA ; trans-cinnamic acid ; TLC ; thin layer chromatography ; L-PM ; L-phenylalanine methyl ester ; t-CM ; trans-cinnamic acid methyl ester
- 刊名：Enzyme and Microbial Technology
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：96
- 期：Complete
- 页码：151-156
- 全文大小：494 K
文摘
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Phenylalanine ammonia lyase (PAL) enzyme activity of Rhodotorula glutinis has been demonstrated in four commonly used ionic liquids.
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Enzyme activity of oligomeric PAL protein in the reaction mixture containing 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]) is comparable to that obtained in aqueous buffer medium.
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Various conditions were standardized for optimal PAL forward activity in the reaction mixture containing [BMIM][PF6]; about 83% conversion of L-phenylalanine to trans-cinnamic acid was obtained.
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PAL reverse activity in ionic liquids was shown for the first time; about 59% conversion of trans-cinnamic acid to L-phenylalanine was obtained in the reaction mixture containing [BMIM][PF6].