Related Experiment Video
Updated: Feb 10, 2026
08:04
Preparation of Functional Silica Using a Bioinspired Method
Published on: August 1, 2018
17.8K
Bioinspired construction of multi-enzyme catalytic systems
Jiafu Shi1, Yizhou Wu, Shaohua Zhang
1Tianjin Engineering Center of Biomass-derived Gas and Oil, School of Environmental Science and Engineering, Tianjin University, Tianjin 300072, China.
Chemical Society Reviews
|May 9, 2018
Summary
Multi-enzyme catalysis offers a sustainable approach to synthesizing valuable chemicals. Strategies like compartmentalization and substrate channeling enhance efficiency for green chemistry applications.
Area of Science:
- Biocatalysis
- Green Chemistry
- Synthetic Biology
Background:
- Enzyme catalysis is a sustainable and efficient process.
- Multi-enzyme catalysis bridges single-enzyme and whole-cell catalysis, crucial for renewable feedstock conversion.
- It plays a vital role in energy and environmental applications.
Purpose of the Study:
- To review recent advances in multi-enzyme catalysis.
- To highlight the strategies of compartmentalization and substrate channeling for constructing multi-enzyme catalytic systems (MECSs).
- To discuss the application of these strategies in in vitro multi-enzyme reactions (MERs).
Main Methods:
- Review of existing literature on enzyme catalysis, compartmentalization, and substrate channeling.
- Analysis of strategies for constructing multi-enzyme catalytic systems (MECSs).
- Examination of in vitro multi-enzyme reactions (MERs) implementation.
Main Results:
- Living organisms utilize compartmentalization and substrate channeling for in vivo multi-enzyme reactions (MERs).
- These strategies are applied to create MECSs with enhanced catalytic activity and stability.
- Both strategies are effective for constructing MECSs for practical biocatalysis.
Conclusions:
- Compartmentalization and substrate channeling are key strategies for developing efficient MECSs.
- Future prospects involve the rational combination of these strategies for advanced biocatalysis.
- This review provides insights into the burgeoning field of multi-enzyme catalysis.
Related Concept Videos
01:07Catalytically Perfect Enzymes
5.1K
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.
Most enzymes...
Most enzymes...
5.1K
01:22Multi-input and Multi-variable systems
428
Cruise control systems in cars are designed as multi-input systems to maintain a driver's desired speed while compensating for external disturbances such as changes in terrain. The block diagram for a cruise control system typically includes two main inputs: the desired speed set by the driver and any external disturbances, such as the incline of the road. By adjusting the engine throttle, the system maintains the vehicle's speed as close to the desired value as possible.
In the absence of...
In the absence of...
428
02:34Enzymes
95.1K
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...
95.1K
01:19Turnover Number and Catalytic Efficiency
21.7K
The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
21.7K
01:19Enzyme Kinetics
104.3K
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
104.3K
02:13Reduction of Alkenes: Catalytic Hydrogenation
14.2K
Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
14.2K