Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Enzymes02:34

Enzymes

92.2K
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...
92.2K
Introduction to Enzymes01:22

Introduction to Enzymes

30.5K
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...
30.5K
The Proteasome Structure01:17

The Proteasome Structure

1.5K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
1.5K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.8K
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...
4.8K
The Proteasome02:18

The Proteasome

9.9K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
9.9K
The Proteasome01:13

The Proteasome

1.5K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Hypocretin-1/ Orexin-A fragment1-16 as a potential surrogate marker for diagnosing narcolepsy type 1.

Sleep·2026
Same author

Bumped Kinase Inhibitor BKI-1708 Interferes in Cytokinesis and Drives Baryzoite Conversion in the Cyst-Forming Apicomplexan Parasites <i>Toxoplasma gondii</i>, <i>Neospora caninum</i> and <i>Besnoitia besnoiti</i>.

International journal of molecular sciences·2026
Same author

Systemic inflammation triggers local complement production in the mouse retina and RPE.

Journal of neuroinflammation·2026
Same author

Potential Molecular Targets of the Broad-Range Antimicrobial Peptide Tyrothricin in the Apicomplexan Parasite <i>Toxoplasma gondii</i>.

Biomedicines·2026
Same author

The TDG protein environment connects active DNA demethylation with chromatin and RNA biology.

Cellular and molecular life sciences : CMLS·2025
Same author

Pleiotropic Effects on Tachyzoite and Host Cell Proteomes in Knock-Out Clones of the Open Reading Frames 297720 and 319730 Constitutively Expressed in <i>T. gondii</i> ShSp1 Tachyzoites.

International journal of molecular sciences·2025

Related Experiment Video

Updated: Dec 24, 2025

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.4K

Partially shielded enzymes capable of processing large protein substrates.

Manon L Briand1, Remy Gebleux, Federica Richina

  • 1School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland, Hofackerstrasee 30, Muttenz CH-4132, Switzerland. patrick.shahgaldian@fhnw.ch.

Chemical Communications (Cambridge, England)
|April 9, 2020
PubMed
Summary

Researchers developed a novel enzyme protection method for creating partially shielded enzymes. These enzymes efficiently process large substrates like proteins and exhibit enhanced stability and activity, advancing biochemical applications.

More Related Videos

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.2K
Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
19:23

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation

Published on: January 16, 2019

9.6K

Related Experiment Videos

Last Updated: Dec 24, 2025

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.4K
Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.2K
Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
19:23

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation

Published on: January 16, 2019

9.6K

Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Protein Chemistry

Background:

  • Enzymes are crucial biological catalysts with diverse applications.
  • Protecting enzymes from degradation and denaturation is vital for their effective use.
  • Current methods often limit enzyme activity or substrate size.

Purpose of the Study:

  • To develop a novel method for enzyme protection.
  • To create partially shielded enzymes capable of processing large substrates.
  • To evaluate the activity, bioconjugation potential, and stability of these modified enzymes.

Main Methods:

  • Enzyme shielding technique to create partially protected enzyme variants.
  • Assays to measure transpeptidase activity of shielded sortase.
  • Proteolytic kinetics studies on shielded trypsin.
  • Assessment of temporal stability under various conditions.

Main Results:

  • Partially shielded enzymes can process substrates as large as proteins.
  • Shielded sortase retains transpeptidase activity for antibody bioconjugation.
  • Shielded trypsin demonstrates superior proteolytic kinetics compared to soluble trypsin.
  • Partial enzyme shielding significantly enhances enzyme temporal stability.

Conclusions:

  • The developed enzyme protection method allows for the creation of robust, active enzymes.
  • Partially shielded enzymes offer improved performance and stability for biochemical applications.
  • This technology has potential implications for enzyme-based therapeutics and industrial processes.