Related Experiment Video
Updated: May 15, 2026
09:27
Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance.
Liang-Bing Wang1, You-Cheng Wang, Rong He
1Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
Journal of the American Chemical Society
|January 16, 2013
Summary
We designed a novel calcium phosphate-alpha-amylase nanobiocatalyst. This system shows enhanced enzyme activity, stability, and durability due to its structure and allosteric regulation.
Area of Science:
- Biocatalysis
- Nanomaterials Science
- Enzyme Engineering
Background:
- Enzyme immobilization in nanomaterials can enhance catalytic activity.
- Allosteric regulation offers a mechanism to modulate enzyme function.
Purpose of the Study:
- To rationally design a CaHPO(4)-α-amylase hybrid nanobiocatalytic system.
- To investigate the influence of allosteric effects and nanostructure morphology on enzyme activity.
- To evaluate the stability and durability of the designed nanobiocatalyst.
Main Methods:
- Aqueous solution calcification approach to synthesize hybrid nanostructures.
- Preparation of CaHPO(4)-α-amylase nanobiocatalysts with varying morphologies (nanoflowers, nanoplates, hexahedrons).
- Enzymatic performance evaluation of hybrid systems and free α-amylase.
Main Results:
- Successfully synthesized CaHPO(4)-α-amylase hybrid nanobiocatalytic systems with distinct morphologies.
- Demonstrated that allosteric regulation and nanostructure morphology significantly impact enzymatic activity.
- CaHPO(4)-α-amylase hybrid nanoflowers exhibited significantly enhanced catalytic activity.
- The hybrid nanobiocatalyst showed improved stability and durability compared to free enzyme with Ca(2+).
Conclusions:
- The rational design of CaHPO(4)-α-amylase hybrid nanobiocatalysts leverages allosteric effects and hierarchical structures for enhanced performance.
- Hybrid nanoflower structures offer superior catalytic activity, stability, and durability.
- This work provides insights into designing advanced nanobiocatalytic systems.
Related Concept Videos
01:08Allosteric Regulation
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
01:13Introduction 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...
01:13Introduction 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...
01:07Catalytically 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.
02:34Enzymes
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...
01:19Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...