عزل و تنقية بيتا كازين حليب الماعز المحلي و دراسة فعالية متحللاته في تثبيط الإنزيم المحول للأنجيوتنسين 1

Abstract EN

β- Casein (β-CN) protein from the acid casein of local goat milk was purified primarily using concentrations of urea solution and pH change, then purified with negative ion exchanger DEAE-cellulose 52 and gel filtration using column SephadexG-75.

Its purity was confirmed by electrophoresis with SDS-PAGE and the β- CN appeared in a single band with MW of 24.2 kDa estimated by the protein RF measurement method.

The hydrolysis of pure β-CN with pepsin, trypsin, and both together at a 1:1 ratio several peptides appeared in the hydrolysates that differed in their ability to inhibit the angiotensin-converting enzyme 1 (ACE1) and had the highest inhibition of the peptides produced by pepsin and trypsin together, especially after 8 hours of hydrolysis which indicated with symbol (βM8H).

Degree of Hydrolysis (DH) was 54.443 % with inhibition rate is 67.310% comparison of DH 48.701 and 42.23% with inhibition rates of 64.84 and 65.665% for both hydrolysates by pepsin and trypsin respectively