title: Effect of gastric conditions on β-lactoglobulin interfacial networks: influence of the oil phase on protein structure.
abstract: Understanding the effects of digestion conditions on the structure of interfacial protein networks is important in order to rationally design food emulsions which can moderate lipid digestion. This study compares the effect of gastric conditions (pH, temperature, and ionic strength) on β-lactoglobulin films at different fluid interfaces: air-water, tetradecane-water, and olive oil-water. The experiments have been designed to simulate the passage into the stomach media. Hence, preformed interfacial protein (β-lactoglobulin) networks have been exposed to gastric conditions in order to establish generic aspects of the digestion process. The results show that the presence of an oil phase affects both the unfolding of the protein at the interface on adsorption and the subsequent interprotein associations responsible for network formation at the interface. Furthermore, the effects of the physiological conditions characteristic of the stomach also altered differently the preformed protein layer at different fluid interfaces. Initially, the effects of temperature, acid pH, and ionic strength on the dilatational modulus of β-lactoglobulin adsorbed layers at tetradecane-water and olive oil-water interfaces were studied in isolation. The presence of salt was found to have a major effect on the dilatational response at the oil-water interface in contrast to the observations at the air-water interface: it enhanced intermolecular association, hence increasing the packing at the interface causing it to become more elastic. Exposure to acid pH (2.5) also increased the elasticity of the interface, possibly due to the fact that strong electrostatic interactions acting at the interface compensated for the reduced level of intermolecular association. However, the increase in dilatational modulus at the oil-water interface was less noticeable upon exposure to combined changes in acid pH and ionic strength, as would occur in the stomach. This is consistent with previously reported observations at the air-water interface. The quantitative differences in the response of the protein networks to gastric media at different fluid interfaces are discussed in terms of the conformation of β-lactoglobulin within the networks formed at each interface based on detailed theoretical modeling of adsorption data.
authors.affiliation: Institute of Food Research, Norwich Research Park, Norwich NR4 7UA, United Kingdom. julia@ugr.es
authors.forename: Julia
authors.initials: J
authors.lastname: Maldonado-Valderrama
authors.forename: Reinhard
authors.initials: R
authors.lastname: Miller
authors.forename: Valentin B
authors.initials: VB
authors.lastname: Fainerman
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Wilde
authors.forename: Victor J
authors.initials: VJ
authors.lastname: Morris
mesh_terms: D000327:Adsorption; D000818:Animals; D040761:Biomimetic Materials / Q000737:chemistry* / Q000494:pharmacology*; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry*; D009821:Oils / Q000737:chemistry* / Q000494:pharmacology*; D009994:Osmolar Concentration; D011487:Protein Conformation / Q000187:drug effects; D013270:Stomach / Q000737:chemistry*; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D007782:Lactoglobulins; D009821:Oils; D014867:Water