Optimization of extraction ratio (ER) of tree peony seed protein (TPSP) was investigated using response surface methodology (RSM). The second-degree equation for ER of TPSP had high coeffi cient (0.9625) of determination. The probability (P) value of regression model signifi cance was less than 0.001 by analysis of central composite rotatable design. Relationships of ER to pH, liquid/solid ratio, squares of all factors, and cross-product factors (x2x3, x2x4, x3x4) were signifi cant (P<0.05). Whereas, extraction time, temperature, and cross-product terms (x1x2, x1x3, x1x4) were not signifi cant factors (P>0.05). Optimum extraction conditions were 3.42 h, pH 9.50, 50.80 ºC, and 9.54 ml g–1 of liquid/solid ratio with the maximum ER (43.60%) . SDS-PAGE indicated TPSP had mainly four proteins (180, 100, 60, and 35 kDa) with four subunits of 60, 48, 38, and 23 kDa. TPSP had a good amino acid composition with abundant essential amino acids (39.76%) determined by amino acid analysis.
Authors:L.H. Feng, Y.Q. Li, G.J. Sun, and X.Z. Zhao
The objective of this work was to research the antibacterial effects of orange pigment, which was separated from Monascus pigments, against Staphylococcus aureus. The increase of the diameter of inhibition zone treated with orange pigment indicated that orange pigment had remarkable antibacterial activities against S. aureus. Orange pigment (10 mg ml−1) had a strong destructive effect on the membrane and structure of S. aureus by the analysis of scanning electron microscopy as well as transmission electron microscopy. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) further demonstrated that the cell membrane was seriously damaged by orange pigment, which resulted in the leakage of protein from S. aureus cells. A significant decrease in the synthesis of DNA was also seen in S. aureus cells exposed to 10 mg ml−1 orange pigment. All in all, orange pigment showed excellent antibacterial effects against S. aureus.
Authors:Y. Li, F.Q. Lu, Y. Feng, Z.D. He, and X.L. Wu
Analysis of the binding interaction of (−)-epigallocatechin-3-gallate (EGCG) and pepsin is important for understanding the inhibition of digestive enzymes by tea polyphenols. We studied the binding of EGCG to pepsin using fluorescence spectroscopy, Fourier transform infrared spectroscopy, isothermal titration calorimetry, and protein-ligand docking. We found that EGCG could inhibit pepsin activity. According to thermodynamic parameters, a negative ΔG indicated that the interaction between EGCG and pepsin was spontaneous, and the electrostatic force accompanied by hydrophobic binding forces may play major role in the binding. Data from multi-spectroscopy and docking studies suggest that EGCG could bind pepsin with a change in the native conformation of pepsin. Our results provide further understanding of the nature of the binding interactions between catechins and digestive enzymes.