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Related Experiment Video

Updated: Jul 20, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Lipase-catalyzed reactions at different surfaces.

P Reis¹, K Holmberg, T Debeche

¹Nestlé Research Center, CH-1000 Lausanne 26, Switzerland.

Langmuir : the ACS Journal of Surfaces and Colloids

|September 6, 2006

Summary

Surface properties significantly influence enzyme activity. Tailored hydrophobic and hydrophilic surfaces alter lipase-catalyzed reactions, impacting product formation in situ using surface plasmon resonance (SPR).

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

Biocatalysis
Surface Chemistry
Enzyme Immobilization

Background:

Enzyme immobilization is crucial for biocatalysis, affecting enzyme activity and selectivity.
Surface properties play a key role in enzyme-substrate interactions and reaction outcomes.
The surface plasmon resonance (SPR) technique offers real-time monitoring of surface-bound reactions.

Purpose of the Study:

To investigate the impact of tailored surface chemistries on Rhizomucor miehei lipase activity.
To explore the use of SPR for in-situ monitoring of lipase-catalyzed biotransformations.
To understand how surface hydrophobicity/hydrophilicity influences hydrolysis versus condensation reactions.

Main Methods:

Fabrication of three distinct surfaces (hydrophobic, hydrophobic with carboxyl groups, hydrophilic) via self-assembled monolayers.
Immobilization of Rhizomucor miehei lipase onto these surfaces through adsorption or covalent binding.
Monitoring substrate adsorption and in-situ biocatalysis using surface plasmon resonance (SPR).

Main Results:

Lipase immobilized on hydrophilic surfaces favored hydrolysis, producing capric acid from monocaprin.
Lipase on hydrophobic surfaces, especially when covalently bound, favored condensation, producing dicaprin.
SPR was successfully utilized for real-time, in-situ monitoring of lipase-catalyzed reactions.

Conclusions:

Surface chemistry is a critical factor in directing lipase-catalyzed reaction pathways (hydrolysis vs. condensation).
Tailored immobilization strategies can control enzyme selectivity for specific biocatalytic applications.
This study demonstrates the novel application of SPR for in-situ biotransformation analysis.