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Drying treatment can significantly increase the oil yield of tiger nuts, and the full utilization of starch by-products in tiger nut meal is an important aspect of improving its industrial value. Consequently, the effects of roasting, microwave and roasting treatments on the structure, functional properties and in vitro digestive characteristics of tiger nut starch were investigated. The results showed that compared to that of CS (untreated control starch), samples of BS (baked starch), MS (microwaved starch), and RS (roasted starch) showed deeper color, surface cracks, partial aggregation on the granules, and larger particle size. In addition, baking, microwave and roasting treatments all decreased the relative crystallinity and short-range ordering of the tiger nut starch, explaining the decrease in enthalpy in the DSC results, the increase in the stability of the freeze-thaw, the solubility and the swelling. From the rheological analysis of starch, it was found that the gel structure of tiger nut starch decreased after the aforementioned treatments. This indicates that the branched chain starch was damaged, which impacing the digestibility of the starch. Further in vitro digestion tests demonstrated that three drying treatments increased slow-digestible starch and resistant starch content. Among them, microwave drying treatment had a significant effect on the structural and functional properties of the isolated starch of tiger nut. This study aimed to provide theoretical guidance for the comeplete utilization of tiger nut starch. [ABSTRACT FROM AUTHOR]

To promote the rational use of cabozantinib (CBZ), this paper studied the influence of several nutritional supplements on the interaction between CBZ and bovine serum albumin (BSA), an appropriate alternative model for human serum albumin (HSA) that is one of the important transporter proteins in plasma, by fluorescence spectroscopy and UV–vis spectroscopy. The results showed that CBZ could quench the fluorescence of BSA via a dynamic–static quenching process, and the six nutritional supplements did not change the quenching mode of BSA by CBZ. However, all of them could reduce the binding constant of the CBZ–BSA system at 293 K and increase the polarity around tryptophan residues. Among them, nicotinamide and vitamin B12 (VB12) had a greater effect on the binding constants of the CBZ–BSA system. In the meantime, the thermodynamic parameters of the CBZ–BSA system were examined, indicating that the interaction of CBZ with BSA was spontaneous and dominated by hydrophobic forces. Further research discovered that the combining of CBZ with BSA was primarily located within Site I of BSA, and the binding distance r was 2.48 nm. Consequently, while taking CBZ, patients should use VB12 and nicotinamide carefully, which may interfere with the transport of drugs. [ABSTRACT FROM AUTHOR]

To promote the rational use of cabozantinib (CBZ), this paper studied the influence of several nutritional supplements on the interaction between CBZ and bovine serum albumin (BSA), an appropriate alternative model for human serum albumin (HSA) that is one of the important transporter proteins in plasma, by fluorescence spectroscopy and UV-vis spectroscopy. The results showed that CBZ could quench the fluorescence of BSA via a dynamic-static quenching process, and the six nutritional supplements did not change the quenching mode of BSA by CBZ. However, all of them could reduce the binding constant of the CBZ-BSA system at 293 K and increase the polarity around tryptophan residues. Among them, nicotinamide and vitamin B 12 (VB 12 ) had a greater effect on the binding constants of the CBZ-BSA system. In the meantime, the thermodynamic parameters of the CBZ-BSA system were examined, indicating that the interaction of CBZ with BSA was spontaneous and dominated by hydrophobic forces. Further research discovered that the combining of CBZ with BSA was primarily located within Site I of BSA, and the binding distance r was 2.48 nm. Consequently, while taking CBZ, patients should use VB 12 and nicotinamide carefully, which may interfere with the transport of drugs., (© 2022 John Wiley & Sons Ltd.)