Protease-catalyzed esterification of amino acid in water-miscible ionic liquid.
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.
Noritomi
Hidetaka
H
Division of Applied Chemistry, Tokyo Metropolitan University, Minami-Ohsawa, Hachioji, Tokyo, 192-0397, Japan. noritomi@ecomp.metro-u.ac.jp
Nishida
Sachiko
S
Kato
Satoru
S
D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001407:Bacillus / Q000201:enzymology; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D004951:Esterification / Q000187:drug effects; D052578:Ionic Liquids / Q000737:chemistry / Q000494:pharmacology*; D010179:Pancreas / Q000201:enzymology; D020860:Subtilisin / Q000378:metabolism; D014867:Water / Q000737:chemistry
D000596:Amino Acids; D052578:Ionic Liquids; D014867:Water; D010450:Endopeptidases; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D020860:Subtilisin