Abstract: Six strains of Monascus purpureus were isolated from samples collected in Gutian, Fujian. Mixed with stored strains, the protease activity, proteolysis and yield of crude peptide were investigated. Pediococcus pentosaceus 22 227 and M. purpureus 4 422 were the best combinations, and the inhibition rate of angiotensin-I converting enzyme (ACE) was 84.21%. The optimal fermentation conditions were 28℃ with the ratio of strains was 2∶1 for 7 days, the inhibition rate of ACE was the highest 83.13%. The inhibition rate of ACE was 89.75% after separated and purified by dialysis, Sephadex G-25 chromatography and RP-HPLC. The obtained antihypertensive peptide contained 12 types of amino acids, which included hydrophobic amino acids such as alanine, valine and methionine, and accounted for more than 50%. The results showed that ACE inhibitory peptides can maintain good activity even under low temperature, weakly acidic conditions and in the continuous in vitro digestion test process.
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WANG Jiaolin,YUE Tianli,YUAN Yahong. Preparation of antihypertensive peptides from quinoa by fermentation with Monascus and lactic acid bacteria[J]. Food and Fermentation Industries, 2021, 47(21): 217-224.
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