Summary The objective of this research was to investigate the effects of germination on functional and conformational properties as well as the in vitro trypsin digestibility of soy protein isolate (SPI). The influences of germination on the molecular properties of SPI were also evaluated. The germination degraded lipoxygenase, α, α' subunits of β‐conglycinin (7S) and acidic chains of glycinin (11S) of soybean. Concomitantly, the loss of tertiary structures of SPI occurred due to the germination. The trypsin inhibitor activity of germinated SPI presented a decreasing trend, followed by an increase in the growth of hypocotyls. The in vitro trypsin digestibility of germinated SPI followed a consistent trend with the trypsin inhibitor activity. The protein solubility (PS) and emulsifying properties of SPI were improved by the germination, in a hypocotyl length‐dependent manner. The data suggest that some selected functional properties and the in vitro digestibility of soy proteins can be improved by means of the germination.

Etomidate is a unique drug used for induction of general anesthesia and sedation, and is usually used through intravenous injection clinically. Before targeting to the receptor, etomidate binds proteins in blood when it comes into veins. Thus to study the interaction of etomidate and serum albumin would be of great toxicological and pharmacological importance. In this study, the interaction between etomidate and human serum albumin (HSA) was studied using fluorescence spectroscopy, UV-vis absorption spectroscopy, Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) spectroscopy, site maker displacement and molecular modeling methods. Investigations of the binding constant (K = 3.55 × 10(5 )M(-1), 295 K), the number of binding sites (n = 1.16), thermodynamic parameters (ΔG = 3.13 × 10(4 )J·mol(-1), ΔS = 364 J·mol(-1)·K(-1) and ΔH = -6.85 × 10(5 )J·mol(-1)) for the reaction and changes to the binding sites and conformation in HSA in response to etomidate were presented. Results show that etomidate can bind HSA tightly through electrostatic forces, and the protein skeleton conformation and secondary structure changes thereby. This is the first spectroscopic report for etomidate-HSA interactions which illustrates the complex nature of this subject.