Isolation and purification of αs-CN from Sheep milk and measuring the effectiveness of its enzymatic hydrolysis in inhibiting ACE1

Casein is a biologically and physiologically complex fluid that contains proteins, water, fat, lactose, minerals, and vitamins as its principal constituents that might support the treatment of human body. Isolation of casein using urea and salts was used. Then, casein was partially purified using DEAE-Cellulose and Sephadex-G-75. The hydrolysis degree was estimated after incubation with pepsin, trypsin, and a mixture of them. αs-CN was partially purified with one peak after DEAE-cellulose ion exchange and there is also one peak that appeared after the Sephadex G-25 gel filtration technique. The maximum hydrolysis was gained after 8 hours of incubation with hydrolyzing enzymes. αH hydrolysates of αs-casein showed that the inhibition rate reached about 67% after 8 hours of incubation with a mixture of pepsin and trypsin with a hydrolysis concentration of 0.114 μmol. Results showed that casein extracted from sheep milk can be highly purified using both ion exchange and gel filtration chromatography. Hydrolysis of αs-CN produces low molecular weight protein using pepsin and trypsin and a mixture of them. The αs-CN has a high inhibition rate of the angiotensin-converting enzyme (ACE).