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                <title level="j">Colloids and Surfaces B: Biointerfaces</title>
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                  <publisher>Elsevier</publisher>
                  <biblScope unit="volume">143</biblScope>
                  <biblScope unit="pp">97-106</biblScope>
                  <date type="datePub">2016</date>
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              <idno type="doi">10.1016/j.colsurfb.2016.03.032</idno>
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                <term xml:lang="en">milk fat globule</term>
                <term xml:lang="en">liquid phaseu coexistence</term>
                <term xml:lang="en">model lipid monolayer</term>
                <term xml:lang="en">Digestive lipase</term>
                <term xml:lang="en">atomic force microscopy</term>
              </keywords>
              <classCode scheme="halDomain" n="chim.theo">Chemical Sciences/Theoretical and/or physical chemistry</classCode>
              <classCode scheme="halDomain" n="sdv.bbm.bp">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics</classCode>
              <classCode scheme="halDomain" n="phys.phys.phys-chem-ph">Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]</classCode>
              <classCode scheme="vocinrae-old" n="nouveau né">nouveau né</classCode>
              <classCode scheme="vocinrae-old" n="séparation de phase">séparation de phase</classCode>
              <classCode scheme="vocinrae-old" n="digestion">digestion</classCode>
              <classCode scheme="vocinrae-old" n="lipase gastrique">lipase gastrique</classCode>
              <classCode scheme="vocinrae-old" n="lipide du lait">lipide du lait</classCode>
              <classCode scheme="vocinrae-old" n="lipolyse">lipolyse</classCode>
              <classCode scheme="vocinrae-old" n="triglyceride lipase">triglyceride lipase</classCode>
              <classCode scheme="vocinrae-old" n="globule lipidique">globule lipidique</classCode>
              <classCode scheme="vocinrae-old" n="nutrition">nutrition</classCode>
              <classCode scheme="vocinrae-old" n="allegation santé">allegation santé</classCode>
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              <p>The enzymatic lipolysis of complex natural lipoproteic assemblies such as milk fat globules is central in neonatal digestion. This process first requires the rapid adsorption of a lipolytic enzyme, gastric lipase, onto the membrane enveloping the triglyceride substrate before the onset of catalytic activity. The interactions governing lipase adsorption onto this complex lipid/water interface are not fully elucidated. This study was designed to unravel the interactions of recombinant dog gastric lipase (rDGL) with model monolayers presenting liquid-liquid phase coexistence and mimicking the outer leaflet of the milk fat globule membrane. Combining biophysical tools (ellipsometry, tensiometry and atomic force microscopy), it was evidenced that rDGL partitions toward liquid expanded phase and at phase boundaries. rDGL gets adsorbed at several levels of insertion suggesting molecular cooperation that may favor insertion and strongly impacts on the lipid phase lateral organization. The addition of phosphatidylserine, negatively charged, reinforced adsorption; hence besides hydrophobic interactions and as further investigated through surface potential modeling, rDGL adsorption is favored by electrostatic interactions</p>
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