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Increased Chymotrypsin Activity in AOT/Bile Salt Reversed Micelles by Kenneth S. Freeman; Scott S. Lee; Douglas J. Kiserow; Linda B. McGown is a Chemistry article available to read on EtoBox.
What is Increased Chymotrypsin Activity in AOT/Bile Salt Reversed Micelles about?
Enzymatic activity of chymotrypsin in AOT reversed micelles is facilitated by the addition of a bile salt cosurfactant, sodium taurocholate (NaTC). NaTC diversifies the interfacial properties of the reversed micelles and increases their water capacity, resulting in a more favorable environment for enzymatic catalysis. The reaction velocity for the hydrolysis of the substrate N-glutaryl-L-phenylalanine p-nitroanilide (N-GPNA) by chymotrypsin more than doubles when NaTC is added to AOT reversed micelles in heptane. The enzymatic reaction obeys Michaelis-Menten kinetics in AOT/heptane reversed micelles over the range of NaTC concentrations studied and within a concentration range of 0.05-0.30 mM N-GPNA. NaTC causes changes in the enzyme turnover number, k cat , the Michaelis constant, K M , and the catalytic efficiency of the enzyme, k cat /K M , that are generally consistent with increased enzymatic activity. Similar effects are seen in dodecane, suggesting that exchange of reactants and products among aqueous pools is not a rate-limiting factor in this system.
Who reads Increased Chymotrypsin Activity in AOT/Bile Salt Reversed Micelles?
It is typically read by researchers, students, and practitioners in Chemistry.
- Author
- Kenneth S. Freeman; Scott S. Lee; Douglas J. Kiserow; Linda B. McGown
- Publisher
- Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0021-9797)
- Published
- 1998
- Language
- EN
- Field
- Chemistry (Physical Sciences)