Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6488804 | Food Bioscience | 2018 | 30 Pages |
Abstract
In this study, fermented camel milk was prepared using proteolytic Lactobacillus rhamnosus MTCC 5945 (NS4), which was analyzed for X-prolyl-dipeptidyl aminopeptidase activity and Angiotensin I-Converting Enzyme (ACE) inhibitory activity. The growth conditions (inoculation rate and incubation time) for the production of peptides were optimized using OPA method. Fractionated 3â¯kDa, 5â¯kDa and 10â¯kDa permeate and retentate samples were further analyzed for ACE-inhibitory activity under the optimized growth conditions. Furthermore, 3â¯kDa and 10â¯kDa permeate with highest ACE-inhibitory activities and highest percentage of peptides production were subjected to liquid chromatography mass spectrometry and peptide identification using MASCOT software. Novel peptides were identified from fermented camel milk using homology sequence searching in BlastP (NCBI), and Protein information resource database (PIR). The novelty (ACE-inhibitory activity or Antihypertensive activity) of peptides was also confirmed using novelty search in the database of antihypertensive peptides (AHTPDB).
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Authors
Divyang Solanki, Subrota Hati,