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Protease-catalyzed esterification of amino acid in water-miscible ionic liquid

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Abstract

The activity of two proteases in the esterification of N-acetyl-l-phenylalanine with ethanol was examined in the water-miscible ionic liquid, 1-ethyl-3-methylimidazolium trifluoromethanesulfonate ([emim][Tf]). The activity of subtilisin was not only improved 9-fold by changing from a water-miscible organic solvent, acetonitrile, to [emim][Tf], but also was about three times greater than that in a water-immiscible organic solvent, octane. Likewise, the activity of α-chymotrypsin in [emim][Tf] was more effectively enhanced compared with that in a water-miscible or a water-immiscible organic solvent. The water content in [emim][Tf] affected the activity of subtilisin.

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Acknowledgments

The authors thank Shikoku Kasei Co for supplying 1-ethyl-3-methylimidazolium trifluoromethanesulfonate.

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Correspondence to Hidetaka Noritomi.

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Noritomi, H., Nishida, S. & Kato, S. Protease-catalyzed esterification of amino acid in water-miscible ionic liquid. Biotechnol Lett 29, 1509–1512 (2007). https://doi.org/10.1007/s10529-007-9416-4

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  • DOI: https://doi.org/10.1007/s10529-007-9416-4

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