Succinylation of milk proteins: Influence on micronutrient binding and functional indices

The functionality of milk proteins is an important feature used in food industries. Milk proteins are effectively capable of binding divalent metal ions electrostatically. As well, the hydrophobic and hydrophilic domains present in milk proteins make them excellent modules for the site-specific delivery of various bioactive analytes. Apart from vital functional properties, solubility and stability of milk proteins is always a matter of concern. To achieve the potential functional properties and micronutrient binding ability succinylation of proteins gained candidature of interest. Succinylation of milk proteins improves cellular mineral absorption during simulated gastrointestinal and transwell assay, respectively. Succinylation of various types of milk protein concentrates results in improved functional properties and micronutrient binding abilities. In the present review, functional properties, mineral and vitamin binding properties of milk proteins and their fractions are represented in detail along with the influence of the succinylation upon the respective properties of milk proteins and their fractions.