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Related Experiment Videos

Controlling lipase stereoselectivity via the surface pressure

E Rogalska1, S Ransac, R Verger

  • 1Centre National de la Recherche Scientifique, Centre de Biochimie et de Biologie Moleculaire, Marseille, France.

The Journal of Biological Chemistry
|January 15, 1993
PubMed
Summary

This study investigated lipase stereoselectivity using a novel air-water interface method. Low surface pressures boosted stereoselectivity but reduced catalytic activity for all tested lipases.

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Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Surface chemistry

Background:

  • Enzyme stereoselectivity is crucial for chiral synthesis.
  • Lipases are widely used biocatalysts.
  • Understanding enzyme behavior at interfaces is key.

Purpose of the Study:

  • To investigate the stereoselectivity of four lipases (Rhizomucor miehei lipase, lipoprotein lipase, Candida antarctica B lipase, human gastric lipase).
  • To examine lipase activity towards racemic dicaprin at the air-water interface.
  • To develop a method for measuring enantiomeric excess in monomolecular films.

Main Methods:

  • Spreading racemic dicaprin as a monolayer at the air-water interface.
  • Utilizing a newly developed method to measure enantiomeric excess of residual substrate in monomolecular films.

Related Experiment Videos

  • Assessing stereoselectivity and catalytic activity of four different lipases.

    • Main Results:

    • Stereoselectivity of all four lipases was dependent on substrate surface pressure.
    • Low surface pressures significantly enhanced stereoselectivity.
    • Conversely, low surface pressures led to decreased catalytic activity.

    Conclusions:

    • Enzyme stereoselectivity can be modulated by surface pressure.
    • Interface conditions significantly influence lipase performance.
    • The developed method allows for precise analysis of interfacial enzyme enantioselectivity.