Related Experiment Video
Updated: May 3, 2026

08:37
Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
11.9K
[Structural and functional properties of inulinases. Ways to regulate their activity]
Biofizika
|January 25, 2014
Summary
This review analyzes inulinase enzymes from various sources, focusing on their structure, function, and how their environment affects performance. It explores biophysical perspectives for optimizing biotechnological processes using these enzymes.
Area of Science:
- Biochemistry
- Enzymology
- Biotechnology
Context:
- Inulinases are crucial enzymes in biotechnology.
- Understanding their structural and functional properties is key for process optimization.
- Diverse microbial sources produce inulinases with varying characteristics.
Purpose:
- To review the structural and functional properties of inulinases from various producers.
- To analyze the relationship between enzyme structure, function, and microenvironment.
- To discuss the biophysical perspectives of using free and immobilized inulinases in biotechnological processes.
Summary:
- This review examines the molecular and supramolecular organization of inulinases.
- It details how structural conditions and microenvironment influence enzyme functionality.
- The biophysical aspects of employing free and immobilized inulinases in biotechnology are explored.
Impact:
- Provides insights into inulinase structure-function relationships.
- Highlights opportunities for improving biotechnological applications of inulinases.
- Offers a biophysical basis for enzyme immobilization and process design.
Related Concept Videos
Enzyme Inhibition
72.4K
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
72.4K
Regulation of Metabolism
9.1K
Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
9.1K
Allosteric Regulation
53.3K
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...
53.3K
Enzymes
68.9K
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...
68.9K
Inducible Operons: lac Operon
3.1K
The lac operon in Escherichia coli is a model for understanding inducible gene regulation and metabolic flexibility. It integrates local control by lactose and global regulation through catabolite repression, enabling E. coli to preferentially metabolize glucose when available and switch to lactose utilization when glucose is scarce.Structure and Function of the lac OperonThe lac operon contains three structural genes: lacZ (β-galactosidase), lacY (lactose permease), and lacA...
3.1K
Ligand Binding and Linkage
4.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.4K

