4). The best binding percentage was detected for cheese from Correntes (75.47 ± 0.5%) and the lowest for cheese from Capoeiras (61.78 ± 0.65%). The value for Correntes cheese was not different from those obtained for Arcoverde (72.21 ± 0.24%) Cachoeirinha (75.02 ± 0.02%), São Bento do Una (75.41 ± 0.15%), and Venturosa (74.36 ± 0.04%), while the cheese sample from Capoeiras, which showed the lowest value, was not different from those obtained from Arcoverde, Cachoeirinhas and Venturosa, but the difference was significant compared with those obtained

for cheeses from Correntes (p = 0.033) and São Bento do Una (p = 0.026). These results are of great importance, because besides having other properties the “Coalho” cheese FRAX597 can increase find more the bioavailability of zinc in the body, since intestinal absorption of zinc is affected by a great number of dietary factors, which include proteins, calcium, and metal-complexing. Also, this mineral plays a key role in the function of several enzymes, participates in cell division, genetic expression, physiological processes like cellular growth, and development and genetic transcription (Salgueiro et al., 2000).

It has been reported that phosphorylated peptides encrypted in αs1-, αs2- and β-casein may form soluble complexes with minerals such as calcium, iron and zinc at intestinal pH, modulating their bioavailabilities. These peptides, which act as mineral solubilisers and/or carriers, are known as caseinophosphopeptides (CPPs) and can be released “in vitro” or “in vivo” by enzymatic digestion of dairy products or during their processing ( Clare and Swaisgood, 2000 and Meisel and FitzGerald, 2003). Many CPPs contain high polar acidic sequences of three phosphoserines followed by two glutamic acid residues (SpSpSpEE), which are the binding sites for minerals. Moreover, Temsirolimus chemical structure there is evidence that amino acid residues upstream and downstream of this region

are also involved ( Ferraretto, Gravaghi, Fiorilli, & Tettamanti, 2003). Harzer and Kauer (1982), did not detect zinc binding to dephosphorylated casein; the conclusion might be drawn that the bivalent zinc ion is complexed to casein by the negative charge of phosphate groups, which would be in good agreement with the fact that there was no zinc binding to casein at low pH, where the phosphate residues would be protonated. Another important result about the zinc-binding activity of artisanal “Coalho” cheese was that the zinc bound weakly to phosphoserine residues in CPPs, and according to Sato, Noguchi, and Naito (1986), this weak affinity is relevant to nutrition, because zinc and other minerals can be released progressively in the intestinal lumen, allowing greater absorption of zinc. There are no previous reports about antimicrobial activity of “Coalho” cheese.