Whey protein isolate–chitosan interactions: A calorimetric and spectroscopy study

Studies on the interactions between bovine β-lactoglobulin and chitosan at the solid–liquid interface

“…6 agrees well with that observed from UV-Vis spectroscopy in solution studies [21] and is easily explained considering the degree of charge of both biopolymers:…”

“…Considering that the working conditions were chosen to disfavor the formation of weakly attached protein aggregates, the behavior observed in Fig. 5 is direct proof of the strong interactions between ␤-LG and chitosan, which agrees well with that seen in solution studies [21,22].…”

“…4 and 5, indicate that the adsorption of ␤-LG on chitosan occurs mostly in an irreversible way and that no phase transitions to reversibly adsorbed states seem to occur either after a critical time or coverage. This behavior is in agreement with results in solution [21,22] and illustrates the significant amounts of energy involved in ␤-LG-chitosan interacting forces. Table 3 Surface roughness (Rms) a and average height (Hav) a obtained from the 5 m × 5 m (Fig.…”

“…In our recent research we have performed calorimetric, spectroscopic, and rheological solution studies on the interactions between bovine WPI and chitosans (commercial or extracted from Brazilian schrimps) with different molar mass (M) and degree of deacetylation (DD) [21,22]. Those reports unveiled the important role of solution pH, DD, and WPI-chitosan molar ratio on the strength of the resulting interactions.…”

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

“…Numerous approaches have been explored for assessment of BSA-drug interactions, including surface plasmon resonance (Li et al, 2006) and calorimetric (de Souza et al, 2009), spectroscopic (Cui et al, 2008), chromatographic and capillary electrophoresis (CE) (Bertucci et al, 2003). Moreover, in recent years, capillary electrophoresis-frontal analysis (CE-FA) has been established as an effi cient method for studying noncovalent molecular interactions.…”