Interactions between β-lactoglobulin and polyphenols: Mechanisms, properties, characterization, and applications

Abstract

β-lactoglobulins (βLGs) have a wide range of applications in food because of their ability to emulsify, foam, and gel. This makes them good functional additives. However, their performance depends on temperature, pH, and mineral levels, so their functional qualities are limited in particular applications. How polyphenols (PPs) interact with βLG is crucial for the functional characteristics and quality of dietary compounds. In most food systems, a spontaneous interaction between proteins and PPs results in a “protein-PP conjugate,” which is known to affect the sensory, functional, and nutraceutical qualities of food products. The βLG-PP conjugates can be used to enhance the quality of food. This article emphasizes analytical techniques for describing the characteristics of βLG-PP complexes/conjugates. It also goes over the functions of βLG-PP conjugates, including their solubility, thermal stability, emulsifying, and antioxidant qualities. The majority of βLG-PPs interactions is due to non-covalent (H-bonding, electrostatic interactions) or covalent bonds that are mostly caused by βLG or PP oxidation through enzymatic or non-enzymatic mechanisms. Furthermore, the conformation or type of proteins and PPs, as well as environmental factors like pH and temperature, have a significant impact on proteins-PPs interactions. Higher thermal stability, antioxidant activities, and superior emulsifying capabilities of the βLG-PP conjugates make them useful as innovative additives to enhance the quality and functions of food products.