Adsorption of β-lactoglobulin to solid lipid nanoparticles (SLN) depends on encapsulated compounds. (April 2019)

• Record Type: Journal Article
• Authors: Oehlke, Kathleen; Keppler, Julia K.; Milsmann, Johanna; Mayer-Miebach, Esther; Greiner, Ralf; Steffen-Heins, Anja
• Is Part Of: Journal of food engineering. Volume 247(2019)
• Page Start: 144
• Page End: 151
• Publication Date: 2019-04
• Subjects: Solid lipid nanoparticles -- Tocopherol -- Ferulic acid -- Beta-lactoglobulin -- Protein corona -- Protein adsorption; Food industry and trade -- Periodicals; Food -- Analysis -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Analyse -- Périodiques; Aliments -- Recherche -- Périodiques; 664.005
• DOI: 10.1016/j.jfoodeng.2018.12.005
• Languages: English
• ISSNs: 0260-8774

Abstract

Abstract: When carrier systems like solid lipid nanoparticles (SLN) are added to a protein rich food matrix adsorption of protein to the particles alters the surface properties of SLN which in turn can alter the properties of the whole system. Thus, the effect of the SLN composition on the protein adlayer (protein corona) is important to understand. The adsorption of β-lactoglobulin (βLG) to unloaded SLN and SLN loaded with ferulic acid or tocopherol was studied at pH 5.7 and particle:protein ratios of 2:1 to 10:1 (w/w) by centrifugation, AF4 and ultrafiltration (UF). Up to 10% of the βLG was strongly bound to SLN whereas 40–80% of the βLG formed a loose adlayer. The amount of bound βLG was increased by the presence of tocopherol and decreased by the presence of ferulic acid. The adsorbed protein layer thus depends on SLN characteristics governed by encapsulated compounds. Graphical abstract: Image 1 Highlights: βLG was loosely bound to the SLN surface forming a removable, incomplete adlayer. Encapsulated compounds interfere with adsorption of βLG on the SLN surface. Presence of α-tocopherol at the SLN surface enhances protein adsorption. The effect of encapsulated compounds on the βLG adlayer depends on βLG concentration.