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Related Concept Videos

Enzymes02:34

Enzymes

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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...
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Enzyme Kinetics01:19

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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...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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Enzyme Inhibition01:30

Enzyme Inhibition

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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.
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Introduction to Enzymes01:22

Introduction to Enzymes

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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.’
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Self-Assembling All-Enzyme Hydrogels for Flow Biocatalysis.

Theo Peschke1, Patrick Bitterwolf1, Sabrina Gallus1

  • 1Karlsruhe Institute of Technology (KIT), Institute for Biological Interfaces (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.

Angewandte Chemie (International Ed. in English)
|November 1, 2018
PubMed
Summary

Self-assembling enzyme hydrogels enable continuous flow biocatalysis. These novel biocatalysts demonstrate high stereoselectivity and robustness, efficiently regenerating expensive cofactors for chemical production.

Keywords:
enzymesflow biocatalysisimmobilizationmicroreactorsstereoselective reactions

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Area of Science:

  • Industrial Biotechnology
  • Biocatalysis
  • Enzyme Engineering

Background:

  • Continuous flow biocatalysis offers efficient chemical production using immobilized enzymes.
  • Developing robust and self-assembling enzyme systems is crucial for industrial applications.

Purpose of the Study:

  • To construct self-assembling all-enzyme hydrogels for continuous flow biocatalysis.
  • To enhance stereoselectivity and cofactor regeneration in enzymatic reactions.

Main Methods:

  • Genetically fusing tetrameric enzymes (LbADH and GDH) with SpyTag/SpyCatcher domains.
  • Inducing polymerization into porous hydrogels under physiological conditions.
  • Immobilizing hydrogels in microfluidic reactors for biocatalysis.

Main Results:

  • Achieved near quantitative conversion and excellent stereoselectivity in prochiral ketone reduction.
  • Demonstrated high robustness of the enzyme hydrogels under process and storage conditions.
  • Enabled high total turnover numbers for the NADP(H) cofactor through compartment effect.

Conclusions:

  • Self-assembling enzyme hydrogels represent a promising platform for advanced continuous flow biocatalysis.
  • The developed system offers efficient and stable enzymatic chemical synthesis with cofactor retention.
  • This approach facilitates the industrial production of value-added chemicals.