Related Experiment Video
Updated: Jul 3, 2026

09:27
Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Immobilized catalase: deactivation and reactor stability
1Department of Chemical Engineering, Clarkson University, Potsdam, New York 13676, USA.
Biotechnology and Bioengineering
|January 20, 1993
Summary
Continuous flow reactors with immobilized catalase can suddenly fail due to substrate-inhibited reactions. This study examines the catastrophic shift from high to low conversion states in hydrogen peroxide decomposition.
Area of Science:
- Biochemical Engineering
- Chemical Reaction Engineering
Background:
- Continuous flow reactors are crucial in chemical and biochemical processes.
- Enzyme-catalyzed reactions, like hydrogen peroxide decomposition by catalase, can exhibit complex behaviors.
- Substrate inhibition and self-poisoning can lead to reactor instability.
Purpose of the Study:
- To investigate the quasi-steady state behavior of continuous flow reactors with immobilized catalase.
- To analyze the exchange-of-steady-states phenomenon in substrate-inhibited, self-poisoning reactions.
- To examine this phenomenon using experimental data from bovine liver catalase.
Main Methods:
- Investigated quasi-steady state behavior in a continuous flow reactor.
- Studied the decomposition of hydrogen peroxide by immobilized catalase.
- Analyzed experimental evidence for the exchange-of-steady-states phenomenon.
Main Results:
- Identified conditions under which reactors are susceptible to sudden failure.
- Observed catastrophic shifts from high- to low-conversion quasi-steady states.
- Correlated these findings with experimental data for bovine liver catalase.
Conclusions:
- The exchange-of-steady-states phenomenon is a critical consideration for reactor design and operation.
- Understanding substrate-inhibited, self-poisoning reactions is key to preventing catastrophic reactor failure.
- Immobilized catalase reactors demonstrate this instability, highlighting the need for careful process control.
Related Concept Videos
Catalysis
The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
Catalysis
Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...
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...
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...
Catalytically Perfect Enzymes
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Enzymes
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

