Jiang Fangcheng, Chen Chunling, Wang Xinlan, Huang Wenjing, Jin Weiping, Huang Qingrong
Key Laboratory for Deep Processing of Major Grain and Oil, School of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China.
Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, NJ 08901, USA.
Foods. 2022 May 31;11(11):1626. doi: 10.3390/foods11111626.
The aim of the study was to investigate the effects of whey protein isolate (WPI) fibrils entanglement on the stability and loading capacity of WPI fibrils-stabilized Pickering emulsion. The results of rheology and small-angle X-ray scattering (SAXS) showed the overlap concentration (C*) of WPI fibrils was around 0.5 wt.%. When the concentration was higher than C*, the fibrils became compact and entangled in solution due to a small cross-sectional radius of gyration value (1.18 nm). The interfacial behavior was evaluated by interfacial adsorption and confocal laser scanning microscopy (CLSM). As the fibril concentration increased from 0.1 wt.% to 1.25 wt.%, faster adsorption kinetics (from 0.13 to 0.21) and lower interfacial tension (from 11.85 mN/m to 10.34 mN/m) were achieved. CLSM results showed that WPI fibrils can effectively absorb on the surface of oil droplets. Finally, the microstructure and in vitro lipolysis were used to evaluate the effect of fibrils entanglement on the stability of emulsion and bioaccessibility of nobiletin. At C* concentration, WPI fibrils-stabilized Pickering emulsions exhibited excellent long-term stability and were also stable at various pHs (2.0-7.0) and ionic strengths (0-200 mM). WPI fibrils-stabilized Pickering emulsions after loading nobiletin remained stable, and in vitro digestion showed that these Pickering emulsions could significantly improve the extent of lipolysis (from 36% to 49%) and nobiletin bioaccessibility (21.9% to 62.5%). This study could provide new insight into the fabrication of food-grade Pickering emulsion with good nutraceutical protection.
本研究的目的是探讨分离乳清蛋白（WPI）原纤维缠结对WPI原纤维稳定的Pickering乳液的稳定性和负载能力的影响。流变学和小角X射线散射（SAXS）结果表明，WPI原纤维的重叠浓度（C*）约为0.5 wt.%。当浓度高于C时，由于回转半径的横截面值较小（1.18 nm），原纤维在溶液中变得紧密并缠结。通过界面吸附和共聚焦激光扫描显微镜（CLSM）评估界面行为。随着原纤维浓度从0.1 wt.%增加到1.25 wt.%，实现了更快的吸附动力学（从0.13到0.21）和更低的界面张力（从11.85 mN/m到10.34 mN/m）。CLSM结果表明，WPI原纤维可以有效地吸附在油滴表面。最后，利用微观结构和体外脂解来评估原纤维缠结对乳液稳定性和川陈皮素生物可及性的影响。在C浓度下，WPI原纤维稳定的Pickering乳液表现出优异的长期稳定性，并且在各种pH值（2.0 - 7.0）和离子强度（0 - 200 mM）下也稳定。负载川陈皮素后的WPI原纤维稳定的Pickering乳液保持稳定，体外消化表明这些Pickering乳液可以显著提高脂解程度（从36%提高到49%）和川陈皮素生物可及性（从21.9%提高到62.5%）。本研究可为制备具有良好营养保护作用的食品级Pickering乳液提供新的见解。
