Article

Identification of Angiotensin-I-converting inhibitory peptides in goat milk fermented by lactic acid bacteria isolated from fermented foods and breast milk

Yuliana Tandi Rubak1,2, Lilis Nuraida1,3,*, Dyah Iswantini4,5, Endang Prangdimurti1,3
Author Information & Copyright
1Department of Food Science and Technology, IPB University (Bogor Agricultural University), IPB Dramaga Campus, Bogor 16680, Indonesia.
2Agrotechnology study program, Faculty of Agriculture, Universitas Nusa Cendana Kupang, UNDANA Lasiana Campus, Kelapa Lima, Nusa Tenggara Timur (NTT), Kupang 85228, Indonesia.
3Southeast Asian Food and Agricultural Science and Technology (SEAFAST) Center, IPB University (Bogor Agricultural University), IPB Dramaga Campus., Bogor 16680, Indonesia.
4Department of Chemistry, IPB University (Bogor Agricultural University), IPB Dramaga Campus. , Bogor 16680, Indonesia.
5Tropical Biopharmaca Research Center, IPB University (Bogor Agricultural University), IPB Taman Kencana Campus., Bogor 16128, Indonesia.
*Corresponding Author: Lilis Nuraida, Department of Food Science and Technology, IPB University (Bogor Agricultural University), IPB Dramaga Campus., Bogor 16680, Indonesia. & Southeast Asian Food and Agricultural Science and Technology (SEAFAST) Center, IPB University (Bogor Agricultural University), IPB Dramaga Campus., Bogor 16680, Indonesia. Phone: +62-251- 862-6725. E-mail: lnuraida@apps.ipb.ac.id.

© Copyright 2021 Korean Society for Food Science of Animal Resources. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Mar 16, 2021 ; Revised: Sep 08, 2021 ; Accepted: Sep 25, 2021

Published Online: Oct 07, 2021

Abstract

In this study, the inhibitory activity of Angiotensin-I-Converting Enzyme (ACEI) was evaluated in fermented goat milk fermented by lactic acid bacteria (LAB) from fermented foods and breast milk. Furthermore, the potential for ACEI peptides was identified of fermented goat milk with the highest ACEI activity. The proteolytic specificity of LAB was also evaluated. The 2% isolate was inoculated into reconstituted goat milk (11% w/v), then incubated at 37 °C until pH 4.6 was reached. The supernatant produced by centrifugation was analyzed for ACEI activity and total peptide. Viable counts of LAB and titratable acidity were also evaluated after fermentation. Peptide identification was carried out using Nano LC/MS/MS, and potential as an ACEI peptide was carried out based on a literature review. The result revealed that ACEI activity was produced in all samples (20.44-60.33%). Fermented goat milk by Lc. lactis ssp lactis BD17 produced the highest ACEI activity (60.33%; IC50 0.297 ± 0.10 mg/mL) after 48 h incubation, viable counts >8 Log CFU/mL, and peptide content 4.037 ± 0.27/mL. A total of 261 peptides were released, predominantly casein (93%). The proteolytic specificity of Lc. lactis ssp lactis BD17 through cleavage on the amino acid tyrosine, leucine, glutamic acid, and proline. A total of 21 peptides were identified as ACEI peptides. This study showed that one of the isolates from fermented food, namely Lc. lactis ssp lactis BD17, has the potential as a starter culture for the production of fermented goat milk which has functional properties as a source of antihypertensive peptides.

Keywords: ACE inhibitory activity; antihypertensive peptides; goat milk fermented; proteolytic specificity; Lactococcus lactis ssp lactis BD17


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Special Issue: 67th ICoMST 2021


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