ABSTRACT
To compare the bioavailability of protein-binding zinc, we investigated the impact of baking on the structure of zinc-binding proteins. The results showed that zinc-binding proteins enriched in zinc with relative molecular weights distributed at 6 kDa and 3 kDa. Protein-binding zinc is predisposed to separate from proteins' interiors and converge on proteins' surface after being baked, and its structure tends to be crystalline. Especially -COO, -C-O, and -C-N played vital roles in the sites of zinc-binding proteins. However, baking did not affect protein-binding zinc's bioavailability which was superior to that of ZnSO4 and C12H22O14Zn. They were digested in the intestine, zinc-binding complexes that were easily transported and uptaken by Caco-2 cells, with transport and uptake rates as high as 62.15% and 15.85%. Consequently, baking can alter the conformation of zinc-binding proteins without any impact on protein-binding zinc's bioavailability which is superior to that of ZnSO4 and C12H22O14Zn.
