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Following the structural changes of triolein films during lipolysis

Humphreys, Ben A. LU ; Gutfreund, Philipp ; McCluskey, Andrew R. ; Arnold, Thomas ; Vind, Jesper and Nylander, Tommy LU (2026) In Soft Matter 22(2). p.343-354
Abstract

A major challenge hampering the industrial and biological exploitation of lipases is the self-limiting effect of the lipolytic reaction. Defying sustained attention throughout history, the influence of lipase catalysed lipolysis on the internal structure of thin triglyceride films has proved elusive. An in-depth understanding of the lipolysis process at the triglycerides/aqueous interface will assist in creating innovative methods to enhance yields. This study furthers our understanding of the influence of solution pD (pH equivalent for aqueous solutions prepared with D2O) on the effect of lipolysis on the structure of thin triolein films. All experiments were performed at pD 7.0 or pD 8.5, either side of the apparent... (More)

A major challenge hampering the industrial and biological exploitation of lipases is the self-limiting effect of the lipolytic reaction. Defying sustained attention throughout history, the influence of lipase catalysed lipolysis on the internal structure of thin triglyceride films has proved elusive. An in-depth understanding of the lipolysis process at the triglycerides/aqueous interface will assist in creating innovative methods to enhance yields. This study furthers our understanding of the influence of solution pD (pH equivalent for aqueous solutions prepared with D2O) on the effect of lipolysis on the structure of thin triolein films. All experiments were performed at pD 7.0 or pD 8.5, either side of the apparent pKa of the primary product of the hydrolysis (oleic acid/oleate). Spectroscopic ellipsometry measurements were employed to kinetically track the changes in thickness of the triolein film after the introduction of 2 ppm Thermomyces lanuginosus lipase (TLL). Neutron reflectometry experiments revealed the internal structure of the thin films before and after TLL digestion, while fast kinetic measurements capturing changes to the reflectivity profile throughout lipolysis. Both techniques revealed significant variations in the physical properties and enzymatic conversion of the triolein films between pD 7.0 and pD 8.5.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Soft Matter
volume
22
issue
2
pages
12 pages
publisher
Royal Society of Chemistry
external identifiers
  • pmid:41363988
  • scopus:105025112703
ISSN
1744-683X
DOI
10.1039/d5sm00820d
language
English
LU publication?
yes
id
3ccb3539-a10c-489f-a9b0-5905e9b77281
date added to LUP
2026-03-10 10:37:15
date last changed
2026-09-24 13:58:06
@article{3ccb3539-a10c-489f-a9b0-5905e9b77281,
  abstract     = {{<p>A major challenge hampering the industrial and biological exploitation of lipases is the self-limiting effect of the lipolytic reaction. Defying sustained attention throughout history, the influence of lipase catalysed lipolysis on the internal structure of thin triglyceride films has proved elusive. An in-depth understanding of the lipolysis process at the triglycerides/aqueous interface will assist in creating innovative methods to enhance yields. This study furthers our understanding of the influence of solution pD (pH equivalent for aqueous solutions prepared with D<sub>2</sub>O) on the effect of lipolysis on the structure of thin triolein films. All experiments were performed at pD 7.0 or pD 8.5, either side of the apparent pK<sub>a</sub> of the primary product of the hydrolysis (oleic acid/oleate). Spectroscopic ellipsometry measurements were employed to kinetically track the changes in thickness of the triolein film after the introduction of 2 ppm Thermomyces lanuginosus lipase (TLL). Neutron reflectometry experiments revealed the internal structure of the thin films before and after TLL digestion, while fast kinetic measurements capturing changes to the reflectivity profile throughout lipolysis. Both techniques revealed significant variations in the physical properties and enzymatic conversion of the triolein films between pD 7.0 and pD 8.5.</p>}},
  author       = {{Humphreys, Ben A. and Gutfreund, Philipp and McCluskey, Andrew R. and Arnold, Thomas and Vind, Jesper and Nylander, Tommy}},
  issn         = {{1744-683X}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{2}},
  pages        = {{343--354}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Soft Matter}},
  title        = {{Following the structural changes of triolein films during lipolysis}},
  url          = {{http://dx.doi.org/10.1039/d5sm00820d}},
  doi          = {{10.1039/d5sm00820d}},
  volume       = {{22}},
  year         = {{2026}},
}