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 alpha-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.
Protease-catalyzed esterification of amino acid in water-miscible ionic liquid. Publishing Authors By Initials
Protease-catalyzed esterification of amino acid in water-miscible ionic liquid. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Biotechnology letters
VOLUME: 29
Page Numbers: 1509-12
Journal Abbreviation: Biotechnol. Lett.
ISSN: 0141-5492
DAY: 7
MONTH: 08
YEAR: 2007
Protease-catalyzed esterification of amino acid in water-miscible ionic liquid. Information
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LANGUAGE: eng
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Grant and Affiliation Information for Protease-catalyzed esterification of amino acid in water-miscible ionic liquid.
AFFILIATION: Division of Applied Chemistry, Tokyo Metropolitan University, Minami-Ohsawa, Hachioji, Tokyo, 192-0397, Japan. noritomi@ecomp.metro-u.ac.jp
Country: Netherlands
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MEDLINETA: Biotechnol Lett
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