Abstract
Biologically active peptides from milk whey, such as caseinomacropeptide (CMP), are of great interest for food technology and for the development of new functional foods. CMP is the soluble derivative of k-casein, generated by the cleavage of the enzyme chymosin enzyme in manufacture of cheese. The objective of this work was to isolate the CMP from whey and characterize. The method applied was the ultrafiltration membrane 50, 30 and 5 kDa. The fraction of CMP isolated consisted of 73.7% protein content, 12% lactose and 2.5% sialic acid. The fractions R30, R5R30 and SPD presented chromatographic profiles compatible with CMP by high performance liquid chromatography (HPLC). Process parameters and characteristics of the raw material can change the efficiency of CMP insolation.
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