These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Increased Chymotrypsin Activity in AOT/Bile Salt Reversed Micelles.
    Author: Freeman KS, Lee SS, Kiserow DJ, McGown LB.
    Journal: J Colloid Interface Sci; 1998 Nov 15; 207(2):344-348. PubMed ID: 9792778.
    Abstract:
    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, kcat, the Michaelis constant, KM, and the catalytic efficiency of the enzyme, kcat/KM, 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. Copyright 1998 Academic Press.
    [Abstract] [Full Text] [Related] [New Search]