Unsupplemented acid goat whey containing 0.96% protein and 2.76% lactose was fermented aerobically with 32 microflora extracted from various raw milk cheeses and dairy products. These microflora were screened for their ability to hydrolyse whey proteins (alpha-lactalbumin and/or beta-lactoglobulin) and to generate peptides inhibitors of Angiotensin I Converting Enzyme. Five microflora were able to degrade whey protein. The most efficient microflora was able to fully hydrolyse alpha-lactalbumin and to a lesser extend beta-lactoglobulin. It was extracted from Bamalou des Pyrenées cheese. Micro-organisms involved consisted of yeast Kluyveromyces marxianus and lactobacillus Lactobacillus rhamnosus. Both were able to produce ACE inhibitory peptides after whey fermentation.

Angiotensin-I-Converting Enzyme (ACE) inhibitors peptides were produced from unsupplemented acid goat whey fermented aerobically for 168 h by Kluyveromyces marxianus and Lactobacillus rhamnosus. This yeast-lactobacillus association is GRAS. Two novel lactokinins were identified: NYW and W with IC50 of 20 and 0.86 mum respectively. They both were resistant toward simulated gastrointestinal digestion. In addition, WLAHK was found in the hydrolysate. These three sequences belong to f(99-110) of alpha-la which seems to be a lactokinin cryptic zone. W was the major molecule released by the fermentation process. Considering that W is the precursor of serotonin, the hydrolysate produced could be of interest for the generation of functional health ingredient involved in regulation of affective disorders and hypertension.

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