NDLI: Cationic Reverse Micelles Create Water with Super Hydrogen-Bond-Donor Capacity for Enzymatic Catalysis: Hydrolysis of 2-Naphthyl Acetate by α-Chymotrypsin

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Cationic Reverse Micelles Create Water with Super Hydrogen-Bond-Donor Capacity for Enzymatic Catalysis: Hydrolysis of 2-Naphthyl Acetate by α-Chymotrypsin

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Cationic Reverse Micelles Create Water with Super Hydrogen-Bond-Donor Capacity for Enzymatic Catalysis: Hydrolysis of 2-Naphthyl Acetate by α-Chymotrypsin

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Correa, N. Mariano Mejuto, J. C. Moyano, Fernando Falcone, R. Dario Silber, Juana J.
Description	Author Affiliation: Moyano F ( Departamento de Química, Universidad Nacional de Río Cuarto, Agencia Postal # 3. C.P. X5804BYA Río Cuarto, Argentina.)
Abstract	Reverse micelles (RMs) are very good nanoreactors because they can create a unique microenvironment for carrying out a variety of chemical and biochemical reactions. The aim of the present work is to determine the influence of different RM interfaces on the hydrolysis of 2-naphthyl acetate (2-NA) by α-chymotrypsin (α-CT). The reaction was studied in water/benzyl-n-hexadecyldimethylammonium chloride (BHDC)/benzene RMs and, its efficiency compared with that observed in pure water and in sodium 1,4-bis-2-ethylhexylsulfosuccinate (AOT) RMs. Thus, the hydrolysis rates of 2-NA catalyzed by α-CT were determined by spectroscopic measurements. In addition, the method used allows the joint evaluation of the substrate partition constant $K_{p}$ between the organic and the micellar pseudophase and the kinetic parameters: catalytic rate constant $k_{cat},$ and the Michaelis constant $K_{M}$ of the enzymatic reaction. The effect of the surfactant concentration on the kinetics parameters was determined at constant $W_{0}=[H_{2}O]/[surfactant],$ and the variation of $W_{0}$ with surfactant constant concentration was investigated. The results show that the classical Michaelis–Menten mechanism is valid for α-CT in all of the RMs systems studied and that the reaction takes place at both RM interfaces. Moreover, the catalytic efficiency values $k_{cat}/K_{M}$ obtained in the RMs systems are higher than that reported in water. Furthermore, there is a remarkable increase in α-CT efficiency in the cationic RMs in comparison with the anionic system, presumably due to the unique water properties found in these confined media. The results show that in cationic RMs the hydrogen-bond donor capacity of water is enhanced due to its interaction with the cationic interface. Hence, entrapped water can be converted into “super-water” for the enzymatic reaction studied in this work.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	29
Volume Number	16
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2010-08-02
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Chymotrypsin Chemistry Micelles Naphthols Catalysis Cations Hydrogen Bonding Hydrolysis Molecular Structure Surface Properties Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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