A biodegradable polyester resin was polymerized from N-benzyloxycarbonylL -glutamic acid and ethylene glycol. Rhizopus delemar lipase was used as a biocatalyst for the rupture of ester bonds during the hydrolysis studies. Depolymerization was observed to followa Michaelis–Menten mechanism, with the maximumrate of monomer formation dP/dtmax = 1.12 x 10-8 mol/s and the rate constant Km x 2.03 x 1...

Enzymatic inhibition is one of the key regulatory mechanisms in cellular metabolism, especially enzymatic competitive by product. This process helps cell regulate activities. In this paper, we derive a mathematical model describing The consists coupled system nonlinear ordinary differential equations for species interest. Using nondimensionalization analysis, formula product formation rate mech...

Enzyme kinetics are usually described by the Michaelis-Menten equation, where the time-dependent decrease of substrate (-dS/dt) is a hyperbolic function of maximal velocity (Vmax), Michaelis constant (Km), and amount of substrate (S). Because the Michaelis-Menten function in its most general meaning requires an assumption of steady-state, it is less curvilinear than true enzyme kinetics. A satu...

This article studies a discrete-time Leslie-Gower two predator-one prey system with Michaelis-Menten type harvesting. Positivity and boundedness of the model solution are investigated. Existence stability fixed points examined. Using an iteration scheme comparison principle difference equations, we find out sufficient condition for global positive point. It is shown that criterion Neimark-Sacke...

The reactivity of tyrosinase adsorbed on nanogold bound with 4,4'-bis(methanethiol)biphenyl monolayer self-assembled on a gold disk with catechol in a dipolar aprotic solvent, acetonitrile (AN), was studied by cyclic voltammetric and amperometric methods. Tyrosinase exhibited characteristics of a Michaelis-Menten kinetic mechanism. The tyrosinase attached to the nanogold continued to react with...

The action of a biosensor containing non Michaelis-Menten enzyme was modeled at mixed enzyme kinetics and external diffusion limitation in the case of substrate inhibition. The calculations show that at the electrode surface multi steady-state concentrations of substrate may be generated if diffusion module is much larger than 1 and the substrate bulk concentration is much bigger than Michaelis...