Proteolytic Profiles and Angiotensin-I Converting Enzyme and α-Glucosidase Inhibitory Activities of Selected Lactic Acid Bacteria

2008 ◽  
Vol 73 (2) ◽  
pp. M75-M81 ◽  
Author(s):  
L. Ramchandran ◽  
N.P. Shah
2007 ◽  
Vol 54 (4) ◽  
pp. 160-166 ◽  
Author(s):  
Jin Shan ◽  
Yuka Ogawa ◽  
Takao Watanabe ◽  
Riichiro Morimoto ◽  
Shoko Oota ◽  
...  

2016 ◽  
Vol 88 (3) ◽  
pp. 507-516 ◽  
Author(s):  
Shiro Takeda ◽  
Hisashi Matsufuji ◽  
Koji Nakade ◽  
Shin-ichi Takenoyama ◽  
Abdulatef Ahhmed ◽  
...  

2015 ◽  
Vol 6 (2) ◽  
pp. 622-629 ◽  
Author(s):  
Xin Rui ◽  
Delan Wen ◽  
Wei Li ◽  
Xiaohong Chen ◽  
Mei Jiang ◽  
...  

The present study was conducted to explore a novel strategy to enhance angiotensin I-converting enzyme (ACE) inhibitory activities of navy bean by preparation of navy bean milk (NBM) which was then subjected to fermentation of four lactic acid bacteria (LAB) strains.


2020 ◽  
Vol 13 (2) ◽  
pp. 345-353 ◽  
Author(s):  
Yuliana Tandi Rubak ◽  
Lilis Nuraida ◽  
Dyah Iswantini ◽  
Endang Prangdimurti

Background and Aim: 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. Materials and Methods: 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. Results: 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 Lactobacillus delbrueckii BD7, Lactococcus lactis ssp. lactis BD17, and Lactobacillus kefiri YK4 and JK17, with the highest activity of ACE-I produced by L. kefiri YK4 (IC50 0.261 mg/mL) and L. kefiri JK17 (IC50 0.308 mg/mL). Results of peptide identification showed that L. kefiri YK 4 could release as many as 1329, while L. kefiri JK 17 could release 174 peptides. The peptides produced were 95% derived from casein. The other peptides were from α-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%). Conclusion: L. kefiri YK4 and JK17 are the potential to be used as starter cultures to produce the bioactive peptide as ACE-I in fermented milk.


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