Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Nonlinear Pharmacokinetics: Michaelis-Menten Equation01:18

Nonlinear Pharmacokinetics: Michaelis-Menten Equation

The Michaelis–Menten equation is a fundamental model for describing capacity-limited kinetics in drug metabolism. It offers insights into the rate of decline of plasma drug concentration Cp over time, with Vmax and KM as pivotal parameters.
Vmax represents the maximum achievable process rate, while KM, known as the Michaelis constant, signifies the drug concentration at which the process rate reaches half its maximum. This relationship between Vmax, KM, and Cp gives rise to three distinct...
Pharmacodynamic Models: Emax Drug–Concentration Effect Model01:18

Pharmacodynamic Models: Emax Drug–Concentration Effect Model

The Emax drug-concentration effect model is central to pharmacodynamics in drug discovery and development. This model is predicated on the receptor occupancy theory, which posits that the effect of a drug is directly related to the number of receptors occupied by the drug and the resultant complex formation.The model describes the reversible interaction between a drug (C) and a receptor (R) to form a drug-receptor complex (RC). The kinetics of this interaction are quantified by an equation that...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Transient increase of the energy gap of superconducting NbN thin films excited by resonant narrow-band terahertz pulses.

Physical review letters·2013
Same author

Toxicity and antioxidant activity in vitro and in vivo of two Fucus vesiculosus extracts.

Journal of agricultural and food chemistry·2008
Same author

Extended sphere method for complete investigation of the phase-matching properties of sum- and difference-frequency generation.

Applied optics·2008
Same author

Gout: radiographic findings mimicking infection.

Skeletal radiology·2001
Same author

Patterns of music agnosia associated with middle cerebral artery infarcts.

Brain : a journal of neurology·2000
Same author

Spiral computed tomographic angiography--a new technique for evaluation of vascular access in hemodialysis patients.

American journal of nephrology·1998

Related Experiment Video

Updated: Jul 4, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Mathematical model for internal pH control in immobilized enzyme particles.

J K Liou1, I Rousseau

  • 1TNO Division of Technology for Society, TNO Institute of Applied Chemistry, P.O. Box 108, 3700 AC Zeist, The Netherlands.

Biotechnology and Bioengineering
|October 1, 1986
PubMed
Summary

This study presents a mathematical model for pH control using immobilized enzymes, demonstrating effective pH regulation for penicillin acylase (Pen-G) conversion. The model shows high Pen-G conversion (80-90%) is achievable with this enzymatic pH control system.

More Related Videos

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Related Experiment Videos

Last Updated: Jul 4, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Area of Science:

  • Biochemical Engineering
  • Enzyme Kinetics
  • Mathematical Modeling

Background:

  • Immobilized enzymes are crucial for biocatalysis, but their performance can be limited by internal pH changes.
  • Controlling pH within immobilized enzyme particles is essential for optimizing reaction rates and product yields.
  • Enzyme kinetics are complex, influenced by substrate, product inhibition, and pH-dependent parameters.

Purpose of the Study:

  • To develop a mathematical model for internal pH control in immobilized enzyme particles.
  • To investigate the kinetics of coupled enzyme systems, considering mixed-type kinetics and various inhibition mechanisms.
  • To evaluate the performance of an enzymatic pH controller using urease and penicillin acylase for benzylpenicillin (Pen-G) conversion.

Main Methods:

  • Developed a mathematical model for coupled enzyme kinetics within planar, cylindrical, and spherical particles.
  • Incorporated Michaelis-Menten kinetics with uncompetitive substrate inhibition and competitive/noncompetitive product inhibition.
  • Simulated enzyme performance, calculating effectiveness factors and conversion in a continuous stirred-tank reactor (CSTR) at varying enzyme loadings.

Main Results:

  • The model successfully describes pH control in immobilized enzyme systems, particularly with the urease-ammonia-carbon dioxide buffer system.
  • High conversion rates of benzylpenicillin (Pen-G) between 80-90% were predicted.
  • Optimal performance was observed at bulk pH values around 7.5-8.

Conclusions:

  • A robust mathematical model for enzymatic pH control in immobilized enzyme particles has been established.
  • The coupled urease-penicillin acylase system demonstrates effective pH buffering, enabling high Pen-G conversion.
  • This approach offers a promising strategy for optimizing biocatalytic processes requiring precise pH management.