The desulfite mechanism exploration in a mode: Interaction between casein and sulfite by multi-spectrometry

Yang, Kai; Zhou, Cheng; Liao, Caiping; Sun, Juan; Wang, Yan; Guan, Rongfa; Neng, Jing; Sun, Peilong

doi:10.1016/j.lwt.2021.111225

Cited by 6 publications

(1 citation statement)

References 22 publications

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“…1) 29 also, with the use of the equation we observed that kq for complex FLU-β-CN and PIT-β-CN is 1.6×10 13 and 1.45×10 13 M -1 S -1 respectively that is greater than the maximum diffusion collision quenching rate constant (2.0×10 10 M -1 S -1 ), these results indicate that the static quenching effect exists in the system of FLU and PIT with β-CN. 30,31 For the quenching process of β-CN, the binding constant (Kb) of a complex of FLU and PIT with β-CN can be determined by the following equation (3) (Fig. S-2) 27 which is equal 7.96×10 4 and 3.44×10 4 M -1 at 298 K as shown Table 1, respectively.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Binding of β-casein with fluvastatin and pitavastatin

Dezhampanah

Rajabi

2022

JSCS

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In this work, the binding interaction of fluvastatin (FLU) and pitavastatin (PIT) with bovine ?-casein (?-CN) were performed under physiological conditions (pH 7.2) by fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and molecular docking methods. Due to the formation of FLU-?-CN and PIT-?-CN complexes, the intrinsic fluorescence of ?-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-?-CN and PIT-?-CN complexes were 7.96?104 and 3.44?104M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to ?-CN was higher than that for PIT. Molecular modeling showed different binding sites for FLU and PIT on ?-CN. All these experimental results suggest that ?.

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