A power series solution is presented which describes the steady-state concentration profiles for substrate and product molecules in immobilized enzyme systems. Diffusional effects and product inhibition are incorporated into this model. The kinetic consequences of diffusion limitation and product inhibition for immobilized enzymes are discussed and are compared to kinetic behavior characteristic of other types of effects, such as substrate inhibition and substrate activation
AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations wer...
The steady state, nonlinear diffusion equations which describe reactions in constrained enzyme solut...
The influence of mass-transfer limitations on the performance of immobilized a-chymotrypsin operatin...
A power series solution is presented which describes the steady-state concentration profiles for sub...
The process of enzyme immobilization under the diffusion-controlled regime (i.e., fast attachment of...
When immobilized enzyme kinetics are disguised by inter- and intraparticle diffusion effects, an app...
The effect of slow substrate diffusion on the activity, stability, and selectivity of immobilized en...
AbstractIn some immobilized enzyme systems the steady state of substrate concentration may suddenly ...
A mathematical model of an immobilized enzyme system with Michaelis-Menten mechanism for an irrevers...
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for ...
A restricted diffusion model is developed to study the immobilization of enzyme in porous solid supp...
The Michaelis-Menten equation for the kinetics of a simple enzyme-catalyzed reaction is based on the...
1045-1051The kinetics of immobilized enzymes can not be analyzed by means of the simple Michaelis-M...
A general theory is presented in this article for determining the intrinsic rate constants for the m...
The algorithm by Northrup, Allison, and McCammon has been used for two decades for calculating the d...
AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations wer...
The steady state, nonlinear diffusion equations which describe reactions in constrained enzyme solut...
The influence of mass-transfer limitations on the performance of immobilized a-chymotrypsin operatin...
A power series solution is presented which describes the steady-state concentration profiles for sub...
The process of enzyme immobilization under the diffusion-controlled regime (i.e., fast attachment of...
When immobilized enzyme kinetics are disguised by inter- and intraparticle diffusion effects, an app...
The effect of slow substrate diffusion on the activity, stability, and selectivity of immobilized en...
AbstractIn some immobilized enzyme systems the steady state of substrate concentration may suddenly ...
A mathematical model of an immobilized enzyme system with Michaelis-Menten mechanism for an irrevers...
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for ...
A restricted diffusion model is developed to study the immobilization of enzyme in porous solid supp...
The Michaelis-Menten equation for the kinetics of a simple enzyme-catalyzed reaction is based on the...
1045-1051The kinetics of immobilized enzymes can not be analyzed by means of the simple Michaelis-M...
A general theory is presented in this article for determining the intrinsic rate constants for the m...
The algorithm by Northrup, Allison, and McCammon has been used for two decades for calculating the d...
AbstractThe kinetics of complexing inactivation at identical enzyme and inhibitor concentrations wer...
The steady state, nonlinear diffusion equations which describe reactions in constrained enzyme solut...
The influence of mass-transfer limitations on the performance of immobilized a-chymotrypsin operatin...