Insight into the binding characteristics of epigallocatechin-3-O-gallate and alcohol dehydrogenase: Based on the spectroscopic and molecular docking analysis.

Alcohol dehydrogenase (ADH) is one of the pivotal enzymes for alcohol metabolism, which plays an important role in many physiological processes. In this study, the activation effects of epigallocatechin-3-O-gallate (EGCG) on ADH and the characteristics of the interaction were investigated via biochemical method, spectroscopy methods, and molecular docking. The results demonstrated that EGCG significantly increased the catalytic activity of ADH with a 33.33% activation rate and that EGCG blending slightly altered the microenvironment surrounding ADH aromatic amino acids, with an increase in the quantity of ß-sheet and a decrease in the α-helix. Through the thermal stability analysis, it is further shown that the interaction of the two affects the intra-molecular hydrogen bond formation of the protein, and the conformation is partially extended. Besides, a total of 8 residues in ADH participated in the docking with EGCG, among which Asp-227, Lys-231, Glu-234, Gly-365 and Glu-366 participated in the formation of hydrogen bonds. At the same time, EGCG and amino group of Lys-231 form a noncovalent bond through cation-π interaction. In particular, hydrogen bonding was beneficial to keep the stability of EGCG-ADH, which was the primary driver of ADH activity activation. The results supply a new way for EGCG to activate ADH and a theoretical basis for the development of anti-alcoholism products.

Effects of carboxymethyl chitosan on the oxidation stability and gel properties of myofibrillar protein from frozen pork patties.

The effect of carboxymethyl chitosan (CMCH) on the oxidation stability and gel properties of myofibrillar protein (MP) from frozen pork patties was investigated. The results showed that CMCH could inhibit the denaturation of MP induced by freezing. Compared with the control group, the protein solubility was significantly (P < 0.05) increased, while the carbonyl content, the loss of sulfhydryl groups, and the surface hydrophobicity were decreased, respectively. Meanwhile, the incorporation of CMCH could alleviate the influence of frozen storage on water mobility and reduce the water loss. With the increased concentration of CMCH, the whiteness, strength, and water-holding capacity (WHC) of MP gels were significantly improved, in which the maximum value was at addition level of 1 %. In addition, CMCH inhibited the decrease in the maximum elastic (G') value and loss factor (tan δ) value of samples. By scanning electron microscopy (SEM) observation, CMCH stabilized the microstructure of the gel and maintained the relative integrity of the gel tissue. These findings suggest that CMCH could be used as a cryoprotectant to maintain the structural stability of MP in pork patty during frozen storage.