Abstract
Lactoferrin, lysozyme, and gelatin are three common basic proteins known for their ability to interact with acidic proteins (lactoglobulin, ovalbumin, casein, etc.) and form various supramolecular structures. Their basic nature makes them highly promising for interaction with other acidic proteins to form heteroprotein complex coacervation (HPCC) with a wide range of applications. This review extensively examines the structure, properties, and preparation methods of these basic proteins and delves into the internal and external factors influencing the formation of HPCC, including pH, ionic strength, mixing ratio, total protein concentration, temperature, and inherent protein properties. The applications of different HPCCs based on these three basic proteins are discussed, including the encapsulation of bioactive molecules, emulsion stabilization, protein separation and extraction, nanogel formation, and the development of formulas for infants. Furthermore, the challenges and issues that are encountered in the formation of heteroprotein complexes are addressed and summarized, shedding light on the complexities and considerations involved in utilizing HPCC technology in practical applications. By harnessing the basic proteins to interact with other proteins and to form complex coacervates, new opportunities arise for the development of functional food products with enhanced nutritional profiles and functional attributes.
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