Authors:S.F. Wu, W. Qi, Y.F. Wang, R.X. Su, and Z.M. He
Casein peptides with calcium-chelating capacity were rapidly enriched by using a novel ceramic matrix (CM)-based Ti4+-IMAC adsorbent. The ability of calcium-chelating peptides (CCPs) to bind calcium and the physical properties of complexes formed between CCPs and calcium were investigated. Results demonstrated that the amount of calcium bound depended on the degree of hydrolysis (DH) of casein hydrolysates. The highest calcium binding capacity (683 mg g−1) occurred when bovine casein was hydrolysed by pancreatin at a DH of 0.14%, meanwhile, the calcium content of CCPs-Ca complex exhibited the maximum level (134.96 mg g−1). In addition, CCPs showed a higher radical scavenging capacity (50 µg ml−1; 99% inhibition, or an equivalent activity of 9.91×10−3 M Trolox) compared to casein digest. Moreover, Fourier-transform infrared spectroscopy and fluorescence spectroscopy were used to explore the interaction between CPPs and calcium, and the results demonstrated that phosphoserine residues as well as COO- groups of CCPs were involved in the formation of CCPs-Ca complex.
Authors:G.P. Li, D. Zhou, L.N. Kan, Y.W. Wu, J.F. Fan, and J. Ouyang
The inhibitory effects of phytic acid (PA) on the browning of fresh-cut chestnuts and the associated mechanisms of PA on polyphenol oxidase (PPO) and peroxidase (POD) activities were investigated. The enzymatic browning of chestnut surfaces and interiors was suppressed by soaking shelled and sliced chestnuts in a PA solution. The specific activities of PPO and POD extracted from chestnuts declined due to inhibition by PA. PA was determined to be a competitive inhibitor of both PPO and POD by Lineweaver-Burk plots. The binding modes of PA with PPO and POD were analysed by AutoDock 4.2.
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.