Purification and characterization of an alkaline serine protease producing angiotensin I-converting enzyme inhibitory peptide from Bacillus sp. SS103.

An alkaline serine protease that hydrolyzes soybean protein into strong angiotensin I-converting enzyme inhibitory hydrolysates was isolated from alkalophilic Bacillus sp. SS103 and purified. The enzyme was purified by ammonium sulfate precipitation followed by gel filtration, cationic exchange column chromatography, and anionic exchange column chromatography.

Production and characterization of a soy protein-derived angiotensin I-converting enzyme inhibitory hydrolysate.

We have produced a soy protein-derived angiotensin I-converting enzyme (ACE) inhibitory hydrolysate and characterized its activity, physicochemical, and biochemical properties. The final yield of the hydrolysate was 8.47% (protein basis) with an IC50 value for ACE inhibitory activity of 0.