Related Experiment Video
Updated: Jul 4, 2026
09:27
Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Multi-scale features in recent development of enzymic biocatalyst systems.
1Department of Bioproducts and Biosystems Engineering, Biotechnology Institute, University of Minnesota, St. Paul, MN 55108, USA. ping@umn.edu
Applied Biochemistry and Biotechnology
|June 25, 2008
Summary
Understanding how enzymes function across different scales is key for sustainable biotechnology. Research explores multi-scale correlations to improve industrial enzyme applications in challenging environments.
Area of Science:
- Engineering
- Biotechnology
- Biocatalysis
Background:
- The functional relationship between elements at different size scales presents a significant challenge in engineering sciences.
- Recent advancements in computational tools have enabled systematic examination of multi-scale time and size correlations for complex systems.
- Synthetic biotechnology, particularly industrial enzyme technologies, is gaining prominence for efficient and sustainable chemical processing.
Purpose of the Study:
- To address the challenges in adapting industrial enzyme technologies for drug, biochemical, and biorenewable energy sectors.
- To explore the dynamic tackling of enzymic biocatalyst systems at all size levels.
- To investigate the potential for discovering, understanding, and controlling common features that relate biocatalyst functions across different size scales.
Main Methods:
- Molecular level protein engineering and modification.
- Nanoscale structure fabrication and microenvironment manipulation.
- Construction of microchip devices and macroscopic industrial bioreactors.
Main Results:
- Industrial enzymes are being re-examined for performance in non-conventional conditions (organic solvents, extreme pH, temperatures).
- Enzymic biocatalyst systems are being developed across multiple scales, from molecular to macroscopic.
- Current efforts are largely case-to-case, lacking cross-scale correlation considerations.
Conclusions:
- Optimizing industrial enzyme technologies requires addressing challenges in diverse applications and harsh conditions.
- Multi-scale approaches, from protein engineering to bioreactor design, are crucial for advancing biocatalysis.
- Future research should focus on identifying and controlling cross-scale correlations for enhanced biocatalyst performance and predictability.
Related Concept Videos
01:14Scale-Up Processes
The scale-up of microbial fermentation processes is essential in industrial biotechnology, allowing the transition from laboratory-scale experiments to commercial-scale production while aiming to maintain product yield and quality. This process requires meticulous adjustment of equipment design, process parameters, and contamination control strategies to accommodate increasing culture volumes.At the laboratory scale, cultures are typically maintained in 1 to 10-liter glass or autoclavable...
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...
01:22Introduction to Enzymes
The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...