Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8891180 | LWT - Food Science and Technology | 2018 | 27 Pages |
Abstract
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 25â¯Â°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 â¼5% 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-â¯>â¯acid-â¯>â¯salty-â¯>â¯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.
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Food Science
Authors
Manjula Nishanthi, Jayani Chandrapala, Todor Vasiljevic,