Complexation of β‐lactoglobulin with gum arabic: Effect of heat treatment and enhanced encapsulation efficiency

Abstract

Heat treatment is widely used in food industry. Proteins and polysaccharides as important natural polymers in food, under heat treatment, the interactions between them could mediate the conformation and functional properties of proteins. Thermally induced β‐lactoglobulin‐gum arabic complexes (β‐Lg‐GA) were fabricated, and the effect of heat treatment on physicochemical properties of the complexes was systematically investigated. The average particle size of β‐Lg‐GA complexes decreased with temperature increased, at 85°C, a smaller size of 273 nm was obtained. A saturated adsorption of GA was found when mass ratio of β‐Lg/GA was <1:2. At pH = 4.2–7.0, electrostatic attraction between β‐Lg and GA was low and a fairly constant turbidity was observed, the formed composite particles had good stability to the pH value. Through UV, fluorescence, and FTIR spectroscopy, it was found that formation of the nanoparticles relied on thermal denaturation and aggregation of protein, the electrostatic, hydrophobic, and hydrogen bonding interactions between β‐Lg and GA were also important. Scanning electron microscope further indicated β‐Lg and GA had good compatibility, and the complexes had a spherical core–shell structure at molecular level. In addition, these prepared natural nanoparticles by heat treatment show significantly higher encapsulation efficiency for (‐)‐epigallocatechin‐3‐gallate (EGCG) than that of unheated, thus could be used as a promising carrier for biologically active substances.

Acid–Heat-Induced Fabrication of Nisin-Loaded Egg White Protein Nanoparticles: Enhanced Structural and Antibacterial Stability

“…In order to explain this phenomenon, we may need to consider the following: heating promoted more nisin molecules dispersed in the EWP nanoparticle matrix and inhibited the aggregation of their crystals, thus promoting the formation of more amorphous complexes. Similar results have also been reported for biopolymer particles, which were formed by the heating of β-lactoglobulin-gum arabic complexes in the presence of epigallocatechin-3-gallate with enhanced encapsulation efficiency [42]. These findings suggest that the heating process promoted additional noncovalent interactions between EWP and nisin, ultimately enhancing the encapsulation of nisin within EWP nanoparticles.…”

Polysaccharide Nanoparticles from Isatis indigotica Fort. Root Decoction: Diversity, Cytotoxicity, and Antiviral Activity

“…At higher temperatures, the hydrophobic interaction becomes stronger, which led to a more compact structure of the nanoparticles’ structure and the diameter becoming smaller [ 24 ]. In addition, higher temperatures might cause some compositions to separate from nanoparticles and the diameter to become smaller [ 25 ]. Some studies have demonstrated a similar change in β-lactoglobulin/pectin nanoparticle size with increasing temperature [ 26 , 27 ].…”

Tuning alginate β-lactoglobulin complex coacervation by modulating pH and temperature

“…chitosan, gum arabic and carboxymethylcellulose, interact with b-Lg in a similar manner to alginate. [58][59][60] Alginate further interacts with potato and soy proteins in a similar manner to b-Lg. 12,61 We suspect that the sticker-spacer network findings described here are transferable to other AP protein systems, laying the foundation for a global understanding of how to utilize complex coacervation in the future.…”