Competitive binding of maltodextrin and pectin at the interface of whey protein hydrolyzate-based fish oil emulsion under high temperature sterilization: Effects on storage stability and in vitro digestion.

Whey protein hydrolysate (WPH), maltodextrin (MD), low methoxy pectin (LMP) and high methoxy pectin (HMP) were used to study the interface binding under high temperature sterilization conditions (121 °C, 15 min). The effect of competitive binding of MD and pectin with interface protein on the storage stability and gastrointestinal fate of fish oil emulsion was studied. The low-molecular-weight MD and the interface protein undergo a wide range of covalent binding through the Maillard reaction, while a small amount of high-molecular-weight pectin can form a protective shell with the interface protein through electrostatic interaction to inhibit the covalent reaction of MD, which was called competitive binding. However, due to the bridging and depletion flocculation of pectin, the emulsification stability of fish oil emulsion reduced. After 13 days of storage, compared with the particle size of the WPH fish oil emulsion (459.18 nm), the fish oil emulsion added with LMP and HMP reached 693.58 nm and 838.54 nm, respectively. In vitro digestion proved that WPH fish oil emulsion flocculated rapidly in the stomach (1.76 µm), while WPH-MD and WPH-MD-pectin fish oil emulsions flocculated slightly (less than800 nm). WPH-MD-pectin delayed digestion in the gastrointestinal tract, and HMP exhibited a better slow-release effect. This study provides reference for the design of multi-component functional drinks and other bioactive ingredient delivery system.

The complex of whey protein and pectin: Interactions, functional properties and applications in food colloidal systems - A review.

This review describes the mechanism of non-covalent/covalent interaction of whey protein-pectin (WPP) complexes, including electrostatic interaction, steric hindrance, cross-linking and Maillard reaction. The interaction between whey protein and pectin determines the form of the complex in the system, i.e. co-dissolution, precipitation, separation, complex coacervation and compounding. The interaction of WPP is affected by environmental conditions and its own properties, including several factors such as pH, polymer concentration and ratio, temperature, and ionic strength. In addition, the functional properties of WPP complexes are discussed through illustrative examples. The complexes with good emulsification, heat stability, gelling properties and biological activity have promising application prospects. WPP complexes have been widely studied for application in food colloidal systems, including protein beverages, delivery systems for bioactive substances, fat substitutes and food preservation films/coatings. The understanding of the interaction and functional properties of WPP complexes provides theoretical support for the improvement and design of new food colloidal systems.

The interfacial covalent bonding of whey protein hydrolysate and pectin under high temperature sterilization: Effect on emulsion stability.

In this study, the effect of high-pressure steam sterilization (121 °C for 15 min) on whey protein hydrolysate-pectin solutions and emulsions was studied. The interaction and emulsification characteristics of pectin and whey protein concentrate (WPC) were evaluated from the solution system to the emulsion system. Enzymatic hydrolysis of WPC (WPH, 2 % and 8 % degree of hydrolysis) increased the covalent binding with pectin, which reduced the heat-induced aggregation of protein and improved emulsification. The thermodynamic incompatibility between WPC and pectin was not conducive to the covalent bonding under high temperature sterilization and produced serious aggregates, which also made a rapid increase in particle size (up to ∼3 µm), compared to WPH-pectin emulsion (∼ 400 nm). In addition, if emulsion was stirred during the sterilization, the creaming and protein aggregation could be avoided. By comparing low methoxy pectin (LMP) and high methoxy pectin (HMP), it was found that the whey protein-HMP complex had better emulsification stability, and the steric stabilization played a more important role in emulsion stability than the electrostatic repulsion. The changes of whey protein and pectin at the oil-water interface of the emulsion during the sterilization process may provide a reference for the sterilized bioactive ingredient delivery system.