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Following the structural changes of triolein films during lipolysis
Ben A Humphreys1,2,3, Philipp Gutfreund3, Andrew R McCluskey4,5,6
1Physical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, S-221 00 Lund, Sweden.
Soft Matter
|December 9, 2025
Summary
Lipase activity is limited by self-inhibition. This study reveals how solution acidity (pD) affects lipase
Area of Science:
- Biochemistry
- Enzymology
- Surface Chemistry
Background:
- Lipase-catalyzed lipolysis faces self-limiting challenges, hindering industrial applications.
- Understanding lipase action at the triglyceride/aqueous interface is crucial for yield enhancement.
- The structural impact of lipolysis on thin triglyceride films remains poorly understood.
Purpose of the Study:
- To investigate the influence of solution pD on lipolysis-driven structural changes in thin triolein films.
- To elucidate the role of pD relative to the oleic acid/oleate pKa in modulating lipase activity.
Main Methods:
- Spectroscopic ellipsometry was used for real-time kinetic tracking of triolein film thickness changes.
- Neutron reflectometry provided insights into the internal structure of triolein films before and after lipase digestion.
- Fast kinetic measurements captured dynamic changes in the reflectivity profile during lipolysis.
Main Results:
- Significant variations in triolein film physical properties were observed between pD 7.0 and pD 8.5.
- Enzymatic conversion of triolein films by Thermomyces lanuginosus lipase (TLL) differed notably at the two pD values.
- Neutron reflectometry revealed distinct structural alterations in the films post-TLL digestion, dependent on pD.
Conclusions:
- Solution pD significantly impacts the lipolysis of triolein films by TLL.
- The study provides critical insights into the structural consequences of lipase action at different pD values.
- Findings contribute to developing strategies for optimizing lipase-driven processes.
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