2018
DOI: 10.1016/j.molliq.2018.01.014
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Kinetic study of the inhibition of ionic liquids on the trypsin activity

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Cited by 18 publications
(2 citation statements)
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“…Fan et al [38] reported that the inactivation induced by ILs is consistent with reversible, competitive inhibition after investigating the kinetics of trypsin inhibition by various imidazolium-and ammonium-based ILs. After removing the IL, the enzyme can recover its activity ( Figure 2).…”
Section: Current Developments In Enzymatic Reactions In Ilsmentioning
confidence: 96%
“…Fan et al [38] reported that the inactivation induced by ILs is consistent with reversible, competitive inhibition after investigating the kinetics of trypsin inhibition by various imidazolium-and ammonium-based ILs. After removing the IL, the enzyme can recover its activity ( Figure 2).…”
Section: Current Developments In Enzymatic Reactions In Ilsmentioning
confidence: 96%
“…In recent years, ionic liquids (ILs) have been introduced as the solvent in the chemical processes . They have numerous properties, such as nonvolatility, low toxicity, and nonflammability, which increase their applications in catalysis, green chemistry, enzyme and bio‐catalyst, and chemical industries . Moreover, because of the presence of N atom in their structures, some ILs were applied as the solvent for CO 2 capture .…”
Section: Introductionmentioning
confidence: 99%