Monitoring the adsorption and activity of Yarrowia lipolytica LIP2 lipase at a model phospholipid-triolein-water interface using a dynamic drop tensiometer
Abstract
Lipases are interfacial enzymes that often have to bind to and cross phospholipid layers to reach triacylglycerols in dietary emulsions or intracellular lipid droplets. This interaction was studied using a dynamic drop tensiometer, Yarrowia lipolytica YLLIP2 lipase and triolein (TO) drops covered or not with a monolayer of 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) deposited using liposomes. An inactive YLLIP2 variant (S162A) allowed us to study adsorption in the absence of enzyme activity. Surface tension and dilational modulus were estimated from drop shape analysis and sinusoidal variations of drop volume, respectively. Drop compression and expansion allowed the determination of surface pressure/area compression isotherms and the maximum surface pressure above which the lipase was excluded from the interface (max).
Fitting the variation in dilational modulus with surface pressure to the Frumkin-Lucassen's isotherm allowed us to estimate the molecular area of YLLIP2 S162A adsorbed at the interface.
Without POPC, a large molecular area (1328 Å 2 ) was estimated, suggesting conformational changes occurring at the pure TO/water interface. With POPC, the molecular area was 2-fold lower (641 Å 2 ), which was consistent with the modelling of YLLIP2 interaction with a phospholipid monolayer. YLLIP2 S162A showed a stronger interaction with POPC/TO/water (max=22.9 mN/m) than with TO/water (max=13.6 mN/m) interfaces. Using similar conditions but wild-type YLLIP2, lipase activity on TO was estimated from changes in drop area while keeping the surface tension constant. YLLIP2 activity, observed only with POPC, was found to vary with surface pressure with an optimum at 15 mN/m, illustrating the adaptation of the enzyme to specific interfacial properties. The phospholipid barrier around triacylglycerol drops appeared as an essential partner of lipase adsorption and activity.
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BibTeX
@article{benarouche2026monitoring,
title = {{Monitoring the adsorption and activity of Yarrowia lipolytica LIP2 lipase at a model phospholipid-triolein-water interface using a dynamic drop tensiometer}},
author = {Anaïs Benarouche and Goetz Parsiegla and Alain Cagna and Frédéric Carrière},
journal = {Surfaces and Interfaces},
year = {2026},
month = oct,
doi = {10.1016/j.surfin.2026.110909},
url = {https://hal.science/hal-05785964v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Monitoring the adsorption and activity of Yarrowia lipolytica LIP2 lipase at a model phospholipid-triolein-water interface using a dynamic drop tensiometer
AU - Anaïs Benarouche
AU - Goetz Parsiegla
AU - Alain Cagna
AU - Frédéric Carrière
PY - 2026
DA - 2026/10/07
JO - Surfaces and Interfaces
DO - 10.1016/j.surfin.2026.110909
UR - https://hal.science/hal-05785964v1
AB - Lipases are interfacial enzymes that often have to bind to and cross phospholipid layers to reach triacylglycerols in dietary emulsions or intracellular lipid droplets. This interaction was studied using a dynamic drop tensiometer, Yarrowia lipolytica YLLIP2 lipase and triolein (TO) drops covered or not with a monolayer of 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) deposited using liposomes. An inactive YLLIP2 variant (S162A) allowed us to study adsorption in the absence of enzyme activity. Surface tension and dilational modulus were estimated from drop shape analysis and sinusoidal variations of drop volume, respectively. Drop compression and expansion allowed the determination of surface pressure/area compression isotherms and the maximum surface pressure above which the lipase was excluded from the interface (max). Fitting the variation in dilational modulus with surface pressure to the Frumkin-Lucassen's isotherm allowed us to estimate the molecular area of YLLIP2 S162A adsorbed at the interface. Without POPC, a large molecular area (1328 Å 2 ) was estimated, suggesting conformational changes occurring at the pure TO/water interface. With POPC, the molecular area was 2-fold lower (641 Å 2 ), which was consistent with the modelling of YLLIP2 interaction with a phospholipid monolayer. YLLIP2 S162A showed a stronger interaction with POPC/TO/water (max=22.9 mN/m) than with TO/water (max=13.6 mN/m) interfaces. Using similar conditions but wild-type YLLIP2, lipase activity on TO was estimated from changes in drop area while keeping the surface tension constant. YLLIP2 activity, observed only with POPC, was found to vary with surface pressure with an optimum at 15 mN/m, illustrating the adaptation of the enzyme to specific interfacial properties. The phospholipid barrier around triacylglycerol drops appeared as an essential partner of lipase adsorption and activity.
SN - 2468-0230
ER -