化学
分离乳清蛋白粉
乳清蛋白
分子间力
透明质酸
水溶液
水动力半径
凝聚
分子内力
多糖
结晶学
色谱法
立体化学
有机化学
分子
生物
遗传学
胶束
作者
Weigang Zhong,Changqing Li,Mengxue Diao,Yan Mi,Cuina Wang,Tiehua Zhang
标识
DOI:10.1016/j.colsurfb.2021.111758
摘要
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.
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