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 0.048 mg of protein/mL. ACE inhibitory activity remained stable after a 2-hour incubation with gastric enzymes in vitro. These hydrolysates were shown to be competitive inhibitors as evaluated by the Lineweaver-Burk plots. These ACE inhibitory hydrolysates from soy proteins have potential as biofunctional food components, which have an economic advantage over single purified peptides for the treatment of hypertension and may be incorporated into foods with functional benefits.
Cha
Myeonghwa
M
College of Human Nutrition, Kansas State University, Manhattan, Kansas, USA.
Park
Jyung Rewng
JR
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004044:Dietary Proteins / Q000032:analysis*; D004355:Drug Stability; D006868:Hydrolysis; D010194:Pancreatin / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism; D030262:Soybean Proteins / Q000737:chemistry*; D014462:Ultrafiltration
D000806:Angiotensin-Converting Enzyme Inhibitors; D004044:Dietary Proteins; D030262:Soybean Proteins; D010194:Pancreatin; D010434:Pepsin A