Development of whey beverage containing antihypertensive peptides and fermentated with lactic acid bacteria originated from human intestune.

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Cheese whey beverage containing antihypertensive peptides and fermented with lactic acid bacteria originated from human intestine was developed. Cheese whey proteins were hydrolyzed with pepsin, trypsin, chymotrypsin, proteinase K, actinase E, thermolysin and papain, then evaluated on inhibitory activity against angiotensin converting enzyme (ACE). Strong inhibitory activity was generated by proteinase K and thermolysin digestion.The digests were assayed for changes in the blood pressure of spontaneously hypertensive rats (SHR) after gastric intubation. The active peptides were chromatographically isolated from the protease K digest. Five peptides isolated were clarified amino acid sequences and their origin. Chemically synthesized peptides showed the antihypertensive activity against SHR.A tripeptide of Ile- Pro-Ala which was orally administered to SHR was recovered from lung of SHR.The results indicated that the peptide was absorbed from intestine, then move to lung and bind there with ACE.When cheese whey was digested with food additive grade proteases of actinase AS, proteinase A, kokulase P and denatyme Ap, the highest antihypertensive activity against SHR was observed in actinase AS digest. Growth of Lactobacillus acidophilus group lactic acid bacteria in cheese whey is usually poor but it was improved after digestion with proteases. Combination of protease digestion of cheese whey and fermentation with lactic acid bacteria originated from human intestine made possible development of the double functional whey beverage.