A century of enzyme kinetic analysis, 1913 to 2013.

Quantitative full time course analysis of nonlinear enzyme cycling kinetics

Enzyme inhibition due to the reversible binding of reaction products is common and underlies the origins of negative feedback inhibition in many metabolic and signaling pathways. Product inhibition generates non-linearity in steady-state time courses of enzyme activity, which limits the utility of well-established enzymology approaches developed under the assumption of irreversible product rele...

A century of dental education: the Cork University Dental School and Hospital, 1913-2013.

Influence of a Novel Magnetic Recoverable Support on Kinetic, Stability and Activity of Beta-amylase Enzyme

In this paper, covalent immobilization of beta amylase enzyme on the surface of modified magnetic nano particles (ZnFe2O4@SiO2-NH2) is reported. For doing so, at first, the magnetic nanoparticles of ZnFe2O4 were synthesized by chemical co-precipitation method and then tetraethyl orthosilicate (TEOS) and 3-aminopropyltriethoxy sil...

Kinetic Modeling of Enzymatic Hydrolysis of Pretreated Sorghum Bicolor and Rice Husk

In this study, the hydrolysis of pretreated sorghum stem and rice husk was investigated at various initial enzyme concentrations and substrate loadings. The slowdown in enzymatic hydrolysis of lignocellulosic materials with conversion has often been attributed to decreasing the activity of enzyme. A kinetic model was developed and expressed mathematically based on enzyme deactivation for enzyma...

The original Michaelis constant: translation of the 1913 Michaelis-Menten paper.

Nearly 100 years ago Michaelis and Menten published their now classic paper [Michaelis, L., and Menten, M. L. (1913) Die Kinetik der Invertinwirkung. Biochem. Z. 49, 333-369] in which they showed that the rate of an enzyme-catalyzed reaction is proportional to the concentration of the enzyme-substrate complex predicted by the Michaelis-Menten equation. Because the original text was written in G...