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 Experiment Videos

How do lipases and esterases work: the electrostatic contribution.

M T Neves Petersen1, P Fojan, S B Petersen

  • 1Biostructure and Protein Engineering Group, Institute of Life Science, Aalborg University, Sohngaardsholmsvej 57, DK-9000, Aalborg, Denmark.

Journal of Biotechnology
|February 13, 2001
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Release of antimicrobial peptides from electrospun nanofibres as a drug delivery system.

Journal of biomedical nanotechnology·2013
Same author

The degradation of arabinoxylan-rich cell walls in digesta obtained from piglets fed wheat-based diets varies depending on digesta collection site, type of cereal, and source of exogenous xylanase.

Journal of animal science·2013
Same author

Pharmacokinetics following continuous subcutaneous insulin infusion of insulin aspart with or without initial subcutaneous bolus.

Diabetes, obesity & metabolism·2010
Same author

A novel approach to prediction of the 3-dimensional structures of protein backbones by neural networks.

FEBS letters·2009
Same author

An atomic force microscopy study of the interactions between indolicidin and supported planar bilayers.

Journal of nanoscience and nanotechnology·2008
Same author

Role of solvent, pH, and molecular size in excited-state deactivation of key eumelanin building blocks: implications for melanin pigment photostability.

Journal of the American Chemical Society·2008
Same journal

The Effect of Reduced Graphene Oxide in Chitosan-Based Nanoparticles on the Enzymatic Properties of the Immobilized Enzyme.

Journal of biotechnology·2026
Same journal

High-level biosynthesis of gastrodin in engineered Escherichia coli.

Journal of biotechnology·2026
Same journal

From plasmid sequence to process design: A computational analysis of metabolism in the context of plasmid DNA manufacturing.

Journal of biotechnology·2026
Same journal

Development of an inducible cellobiohydrolase promoter and its application for enhancing the production of ganoderic acids in Ganoderma lingzhi.

Journal of biotechnology·2026
Same journal

Malic acid and allied exogenous chemicals induces desaturase gene expression and elevates PUFA production in marine microalgae Isochrysis sp.

Journal of biotechnology·2026
Same journal

Recombinant production of human papillomavirus type 16 E6 and E7 vaccine antigens in Chlamydomonas reinhardtii.

Journal of biotechnology·2026
See all related articles

Electrostatic interactions significantly influence lipase/esterase activity and pH profiles. A negative potential in the active site correlates with triglyceride activity, leading to the proposed

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Lipase/esterase activity is influenced by multiple factors, including electrostatic interactions.
  • The enzyme's pH activity profile is largely determined by the electrostatic potential distribution on its molecular surface as a function of pH.
  • The active cleft's residue composition (polar/hydrophobic) also plays a crucial role.

Purpose of the Study:

  • To investigate the contribution of electrostatic interactions to lipase/esterase activity.
  • To map the electrostatic potential distribution on the surface of nine lipases/esterases as a function of pH.
  • To correlate these potential maps with known pH-activity profiles to understand enzyme function.

Main Methods:

  • Computational mapping of electrostatic potential distribution on the molecular surface of nine lipases/esterases at various pH values.

Related Experiment Videos

  • Comparison of electrostatic potential maps with experimental pH-activity profiles.
  • Analysis of residue distribution (polar, non-polar) within the active site cleft.

    • Main Results:

    • A strong correlation was observed between electrostatic potential maps and enzyme pH-activity profiles.
    • A negative potential in the active site is correlated with maximum activity towards triglycerides.
    • A hypothesis, the 'electrostatic catapult model,' was proposed for product release.
    • Potential roles for charged surface regions in stabilizing phospholipid interactions were suggested for phospholipase-active lipases.

    Conclusions:

    • Electrostatic interactions are a key determinant of lipase/esterase activity and pH dependence.
    • The 'electrostatic catapult model' provides a framework for understanding product release mechanisms.
    • Surface electrostatics and residue distribution are critical for understanding lipolytic and phospholipolytic activities at an atomic level.