Whey protein nanofibrils

  • 文章类型: Journal Article
    由天然聚合物制备的高内相Pickering乳液(HIPPE)在食品制造商中引起了广泛的关注。然而,单一的玉米醇溶蛋白稳定的HIPPE稳定性差,在等电点附近容易絮凝。为了解决这个问题,在这项研究中,玉米醇溶蛋白和乳清蛋白纳米原纤维(WPN)复合纳米颗粒(ZWNP)使用pH驱动方法成功制备,和ZWNP进一步用作HIPPE稳定剂。结果表明,玉米醇溶蛋白和WPN通过氢键和疏水相互作用结合在一起形成ZWNP,ZWNP稳定的HIPPE具有优异的稳定性,能有效保护内包裹的番茄红素,提高番茄红素的生物可及性。总之,本研究为制备稳定的疏水性蛋白基HIPPE提供了一种新策略,以zein为代表。
    High internal phase Pickering emulsions (HIPPEs) prepared from natural polymers have attracted much attention in the food manufactures. However, single zein-stabilized HIPPEs are poorly stable and prone to flocculation near the isoelectric point. To address this issue, in this study, zein and whey protein nanofibrils (WPN) complex nanoparticles (ZWNPs) were successfully prepared using a pH-driven method, and ZWNPs were further used as HIPPEs stabilizers. The results showed that zein and WPN were combined together through hydrogen bonding and hydrophobic interaction to form ZWNPs, and the HIPPEs stabilized by ZWNPs had excellent stability, which could effectively protect the internally encapsulated lycopene and improve the bioaccessibility of lycopene. In conclusion, this study provides a new strategy for the preparation of stable hydrophobic protein-based HIPPEs, represented by zein.
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  • 文章类型: Journal Article
    The application of natural biopolymers to develop colloidal carriers for delivering hydrophobic bioactive molecules has become one of the hottest topics in food science. In this study, a simple pH-driven method to prepare whey protein nanofibrils stabilized zein nanoparticles was developed. The formation, structure, intermolecular interactions, rheological properties, in vitro digestion, and antioxidant activity of the nanoparticles were investigated. When the mass ratio of zein and whey protein nanofibrils was 1:0.8, the hydrodynamic diameter and zeta potential of the nanoparticles were 413 nm and - 25 mV, respectively. Transmission electron microscope photographs showed that the nanoparticles were a spherical core-shell structure. Fourier transform infrared spectroscopy and surface hydrophobicity measurements indicated that whey protein nanofibrils adsorbed to the surface of zein aggregates through hydrogen bonding and hydrophobic interactions. Differential scanning calorimetry tests confirmed the formation of nanoparticles improved the thermal stability of zein and whey protein nanofibrils. The nanoparticles exhibited less shear-thinning behavior with low apparent viscosity, and it can\'t be degraded in simulated gastric fluid but can be in simulated intestinal fluid. The antioxidant activity of the nanoparticles was increased by in vitro antioxidant assay when compared to whey protein nanofibrils. This new technology to develop zein-whey protein nanoparticles may be used for preparing nanoparticles of other similar hydrophobic food ingredients. And the findings of this study may provide a theoretical basis for preparation of nanoparticles as a nutrient delivery system.
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