Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4
Article Abstract:
Research demonstrates production of fermented milks containing angiotensin-I-converting-enzyme-inhibitory peptides by two species of Lactobacillus species. Data on ACE-inhibitory peptide sequences, chemical synthesis, and biological activity are presented.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
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The proteolytic system of Lactobacillus sanfrancisco CB1: purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase
Article Abstract:
The serine proteinase, metal-dependent dipeptidase and a general aminopeptidase are the main proteolytic enzymes responsible for the ability of Lactobacillus sanfrancisco CB1 to degrade peptides during fermentation. The aminopeptidase and the dipeptidase are most active at pH 7.5 and temperature 30 to 35 degree celsius (C). They have a high affinity for peptides with hydrophobic amino acids. The activity of the proteinase is maximum at pH 7.0 and temperature 40 degree C. The proteinase hydrolyzes gliadin rather than casein.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Use of PCR-based methods for rapid differentiation of Lactobacillus delbrueckii subsp. bulgaricus and L. delbrueckii subsp. lactis
Article Abstract:
PCR-based methods for rapid differentiation of Lactobacillus delbrueckii subsp. lactis and L. delbrueckii subsp. bulgaricus and their usage are discussed. PCR was carried out using specific primers designed based on proline iminopeptidase gene sequence data for L. Delbrueckii subsp. bulgaricus.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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