The measurement of values of apparent equilibrium constants ' for enzyme-catalyzed reactions involve a substantial number of critical details, neglect of which could lead to systematic errors. Here, interferences, impurities in the substances used, and failure to achieve equilibrium are matters of substantial consequence. Careful reporting of results is of great importance if the results are to have archival value.
View Article and Find Full Text PDFThe kinetics of enzymatic desymmetrisation were analysed for the most common kinetic mechanisms: ternary complex ordered (prochiral ketone reduction); ping-pong second (ketone amination, diol esterification, desymmetrisation in the second half reaction); ping-pong first (diol ester hydrolysis) and ping-pong both (prochiral diacids). For plausible values of enzyme kinetic parameters, the product enantiomeric excess (ee) can decline substantially as the reaction proceeds to high conversion. For example, an ee of 0.
View Article and Find Full Text PDFThe eQuilibrator component contribution method allows calculation of the overall Gibbs energy changes for conversion of glucose to a wide range of final products in the absence of other oxidants. Values are presented for all possible combinations of products with up to three carbons and selected others. The most negative Gibbs energy change is for the formation of graphite and water (-499 kJ mol) followed by CH and CO (-430 kJ mol), the observed final products of anaerobic digestion.
View Article and Find Full Text PDFACS Appl Mater Interfaces
November 2018
Proteins represent complex biomolecules capable of wide-ranging but also highly specific functionalities. Their immobilization on material supports can enable broad applications from sensing and industrial biocatalysis to biomedical interfaces and materials. We demonstrate the advantages of using aqueous-processed cross-linked polyphenol coatings for immobilizing proteins, including IgG, avidin, and various single and multidomain enzymes on diverse materials, to enable active biofunctional structures (e.
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