Angiotensin-I-converting enzyme inhibitory peptides in milk fermented by indigenous lactic acid bacteria

• Published in: Veterinary World Vol. 13; no. 2; pp. 345 - 353
• Main Authors: Rubak, Yuliana Tandi, Nuraida, Lilis, Iswantini, Dyah, Prangdimurti, Endang
• Format: Journal Article
• Language: English
• Published: India Veterinary World 01.02.2020
• Subjects: Amino acids; Amyloid; Angiotensin; angiotensin-i-converting enzyme inhibitory peptides; Antihypertensives; Casein; Enzymes; Fermentation; fermented milk; Fermented milk products; indigenous lactic acid bacteria; Lactalbumin; Lactic acid; Lactic acid bacteria; lactobacillus kefiri; Mass spectroscopy; Milk; Molecular weight; Peptides; Proteolysis; Starter cultures; β-Lactoglobulin; angiotensin-I-converting enzyme inhibitory peptides; indigenous lactic acid bacteria; fermented milk; Lactobacillus kefiri
• ISSN: 0972-8988; 2231-0916
• DOI: 10.14202/vetworld.2020.345-353

Fermented milk can be used to produce antihypertensive peptides. Lactic acid bacteria (LAB) with its proteolytic system hydrolyze milk protein during fermentation to produce several peptides, which include antihypertensive bioactive peptides. This study aimed to investigate the ability of indigenous LAB for the production of angiotensin-I-converting enzyme inhibitory (ACE-I) peptides in fermented milk and to characterize the ACEI peptides. Reconstituted milk (11%) inoculated with ten LAB isolates, and then incubated at 37°C until it reaches pH 4.6. The evaluation was carried out for LAB count, lactic acid concentration, peptide content, and ACE-I activity. The low molecular weight (MW) peptides (<3 kDa) were identified using Nano LC Ultimate 3000 series system Tandem Q Exactive Plus Orbitrap high-resolution mass spectrometry. The result showed that the ten LAB isolates were able to produce ACE-I in fermented milk with the activities in the range of 22.78±2.55-57.36±5.40%. The activity of ACE-I above 50% produced by BD7, ssp. BD17, and YK4 and JK17, with the highest activity of ACE-I produced by YK4 (IC 0.261 mg/mL) and JK17 (IC 0.308 mg/mL). Results of peptide identification showed that YK 4 could release as many as 1329, while JK 17 could release 174 peptides. The peptides produced were 95% derived from casein. The other peptides were from ά-lactalbumin, β-lactoglobulin, and serum amyloid A. The peptides produced consisted of 6-19 amino acid residues, with MWs of 634-2079 Dalton and detected at 317-1093 m/z. A total of 30 peptides have been recognized based on literature searches as ACE-I peptides (sequence similarity: 100%). YK4 and JK17 are the potential to be used as starter cultures to produce the bioactive peptide as ACE-I in fermented milk.