Using transglutaminase to cross-link complexes of lactoferrin and α-lactalbumin to increase thermal stability.

The poor thermal stability of lactoferrin (LF) hinders its bioavailability and use in commercial food products. To preserve LF from thermal denaturation, complexation with other biopolymers has been studied. Here we present the complex formation conditions, structural stability, and functional protection of LF by α-lactalbumin (α-LA).

Investigating the synergistic effects of high-pressure homogenization and pH shifting on the formation of tryptophan-rich nanoparticles.

A combined treatment of high-pressure homogenization (HPH) and pH-shifting on the mixture of α-lactalbumin (α-LA) and tryptophan (Trp) was used to fabricate nanoparticles (α-LA-Trp-NP). The optimal α-LA/Trp ratio (5:1), HPH pressure (206.8 MPa), and recirculation time (40 min) was found to produce small α-LA-Trp-NP (243.

Synthesis of a Cation-Exchange Resin by Inverse Suspension Polymerization for Lactoferrin Extraction from Whey.

Lactoferrin (LF), the main iron-binding protein of milk, has important nutritional, biological, and pharmaceutical properties. It is an essential nutritional component of newborn diets and also for adult health. Small amounts of lactoferrin can be found in whey, a nutritionally and biologically useful byproduct of the dairy industry.

Encapsulation and stabilization of lactoferrin in polyelectrolyte ternary complexes.

Effective delivery of the bioactive protein, lactoferrin (LF), remains a challenge as it is sensitive to environmental changes and easily denatured during heating, restricting its application in functional food products. To overcome these challenges, we formulated novel polyelectrolyte ternary complexes of LF with gelatin (G) and negatively charged polysaccharides, to improve the thermal stability of LF with retained antibacterial activity. Linear, highly charged polysaccharides were able to form interpolymeric complexes with LF and G, while coacervates were formed with branched polysaccharides.