RESUMEN
In dairy products, the added sodium hyaluronate may form complexes with proteins, thereby affecting product properties. In the present study, the interaction between whey protein isolate (WPI)/ whey protein hydrolysate (WPH) and sodium hyaluronate (SH) was characterized under thermal treatment at different temperatures (25 â, 65 â, 90 â and 121 â) after studying effects of protein/SH ratio and pH on complex formation. The addition of SH reduced the particle size of WPI/WPH and increased potential value in the system, with greater variation with increasing treatment temperature. The structural properties of complexes were studied. The binding with SH decreased the contents of free amino group and free thiol group, as well as the fluorescence intensity and surface hydrophobicity. FTIR results and browning intensity measurement demonstrated the formation of Maillard reaction products. Moreover, the attachment of SH improved the thermal stability of WPI/WPH and decreased their antigenicity.
Asunto(s)
Calor , Ácido Hialurónico , Hidrolisados de Proteína , Proteína de Suero de Leche , Proteína de Suero de Leche/química , Ácido Hialurónico/química , Hidrolisados de Proteína/química , Concentración de Iones de Hidrógeno , Reacción de Maillard , Interacciones Hidrofóbicas e Hidrofílicas , Tamaño de la Partícula , Espectroscopía Infrarroja por Transformada de Fourier , Manipulación de Alimentos/métodosRESUMEN
Complexes of polysaccharides and proteins have superior physicochemical and functional properties compared to single proteins or polysaccharides. In this study, lactoferrin-hyaluronic acid (LF-HA) complexes were prepared by both ultrasonic and thermal treatment. Appropriate preparation conditions, including ultrasonic and thermal treatment conditions, have been established. The complexes formed by different methods were structurally characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis, fourier transform infrared spectroscopy, and circular dichroism spectroscopy. Ultrasound formed non-covalent binding, while thermal treatment generated covalent bonding, altering the structure of LF. The LF-HA complexes showed improved heat stability, foaming stability, emulsifying activity and antioxidant capacity, but deceased foaming ability. Iron binding ability could only be improved by HA through thermal treatment. Moreover, the in vitro digestibility of LF-HA complexes decreased to below 80 % compared to LF.