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Sweet cheese whey has been used to obtain whey cheese without the addition of milk. Pre-treated whey was concentrated by nanofiltration (NF) at different concentration ratios (2, 2.5 and 2.8) or by reverse osmosis (RO) (2-3 times). After the concentration, whey was acidified with lactic acid until a final pH of 4.6-4.8, and heated to temperatures between 85 and 90 °C. The coagulated fraction (supernatant) was collected and freely drained over 4 h. The cheese-whey yield and protein, fat, lactose and ash recoveries in the final product were calculated. The membrane pre-concentration step caused an increase in the whey-cheese yield. The final composition of products was compared with traditional cheese-whey manufacture products (without membrane concentration). Final cheese yields found were to be between 5 and 19.6%, which are higher than those achieved using the traditional 'Requesón' process.

Antihypertensive peptide fraction from whey protein hydrolysate <3 kDa (measured as angiotensin-converting enzyme (ACE) activity %) was isolated and encapsulated into three composite materials: alginate–collagen, alginate Arabic gum, and alginate–gelatin. The release behavior of peptide fraction from capsules was analyzed according to the encapsulation material efficiency, the characteristics of the capsules, and the released antihypertensive peptides during gastrointestinal digestion. The highest encapsulation efficiency was found in capsules of alginate Arabic gum (95%). In this case, the released peptides incremented their ACE activity (85%) after the digestion process, with respect to the initial ACE activity (74%). Whey antihypertensive fraction revealed five peptide sequences; however, other amino acid sequences were released from digested capsules. Protein databases confirmed some antihypertensive sequences indicating the peptides content from β-Lg and α-La. Consequently, new peptides could be revealed from whey antihypertensive fraction.

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