Characterization of interactions between whey protein isolate and hyaluronic acid in aqueous solution: Effects of pH and mixing ratio

[Display omitted] •Detailed phase diagram divided by identified critical pH values as function of mixing ratio was established.•Complexes with ratio above 4:1 in pH window of 3−2 occurred precipitation immediately.•Strongest network was observed at samples at ratio 8:1/pH 2.8.•Mixing biopolymers at certain pH values caused protein conformation change. Interactions between whey protein isolate (WPI) and hyaluronic acid (HA) were characterized as functions of pH (6.0−1.0) and protein to polysaccharide ratio (R, 1:4−10:1). Intramolecular soluble complexes formed at pHc of 5.6–5.8, followed by intermolecular insoluble complexes formed at pHΦ1 of 4.4–4.6. Complexes at ratios below 4:1 reached maximum optical value at pH 2.4 while samples above 4:1 peaked at pH 3–3.4 then precipitated. WPI/HA coacervates completely dissociated into soluble complex at pH 1.6–1.8 (pHΦ2). WPI/HA mixtures showed shear thinning behavior and elastic property. Whey protein underwent significant α-helix structure change when interacting with HA in range of pHΦ1>pH > pHΦ2 and at low R values (1:4 and 1:2). Scanning electronic microscope (SEM) pictures showed pH and mixing ratio dependent microstructural changes corresponding with phase transition. Data may provide helpful information for further application of WPI/HA complexes in medical, food and cosmetic fields.