Catalytic activity of α-chymotrypsin in enzymatic peptide synthesis in ionic liquids |
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| Institution: | 1. Environment Department, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran;2. Center of Excellence in Electrochemistry, Faculty of Chemistry, University of Tehran, Tehran, Iran;3. Biosensor Research Center, Endocrinology & Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran;1. Department of Chemistry, DAV University, Jalandhar, Punjab, India;2. Department of Chemistry, Kurukshetra University, Haryana, India;3. Department of Mathematics, Lyallpur Khalsa College, Jalandhar, Punjab, India;1. Young Researchers and Elite Club, Ahvaz Branch, Islamic Azad University, Ahvaz, Iran;2. Young Researchers and Elite Club, North Tehran Branch, Islamic Azad University, Tehran, Iran;3. Discipline of Chemical Engineering, School of Engineering, University of KwaZulu-Natal, Howard College Campus, King George V Avenue, Durban 4041, South Africa;4. Institut de Recherche en Génie Chimique et Pétrolier (IRGCP), Paris Cedex, France;5. Département de Génie des Mines, de la Métallurgie et des Matériaux, Faculté des Sciences et de Génie, Université Laval, Québec, QC G1V 0A6, Canada |
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| Abstract: | The catalytic activity of α-chymotrypsin in the enzymatic peptide synthesis of N-acetyl-l-tryptophan ethyl ester with glycyl glycinamide was examined in ionic liquids and organic solvents. The water content in 1-ethyl-3-methylimidazolium bis(fluorosulfonyl)imide (emim]FSI]) affected the initial rates of peptide synthesis and hydrolysis. The activity of α-chymotrypsin was influenced by a kind of anions consisting of the same cation, emim], when an ionic liquid was used as a solvent. The initial rate of peptide synthesis was improved 16-fold by changing from an organic solvent, acetonitrile, to an ionic liquid, emim]FSI], at 25 °C. The activity of α-chymotrypsin in the peptide synthesis in emim]FSI] was 17 times greater than that in acetonitrile at 60 °C, although the activity of α-chymotrypsin in the peptide synthesis gradually decreased with an increase in reaction temperature in emim]FSI], similar to organic solvents. Moreover, α-chymotrypsin exhibited activity in emim]FSI] and emim]PF6] at 80 °C. |
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