Storage conditions and composition of whey protein concentrates (WPCs) may destabilize the whey proteins (WPs) thus affect their functionality. Functional characteristics of native, sweet, acid and salty-WPC powders were analyzed after storage at 25 °C and RH (22, 33%) for 90 days. Native-, sweet- and acid-WPCs exhibited high solubility (82–97%), which was largely retained during storage. Solubility of salty-WPC was 52–55% initially, which gradually increased by ?5% during storage. Ionic sodium in salty-WPC interlinked WPs through salt bridges and charge screening, exposing reactive sites for intensive aggregation. Heat stability of salty-WPC was highest (64s), while lowest was recorded for native-WPC (16s). In presence of ionic sodium in salty-WPC, WPs denature due to salt bridging, charge screening and osmotic effects leading to intensive aggregation. High emulsion activity was recorded for salty-WPC, while those for other WPCs were similar. Emulsion stability varied as native- > acid- > salty- > sweet-WPC. High number of hydrophobic segments was likely exposed on the protein surface in salty-WPCs due to sodium-induced WP denaturation, thus increasing the number of proteins absorbed to emulsion interface, enhancing emulsion activity. Functionality of different WPCs during storage predominantly depended on the inherited composition.