ArticleApplied and environmental microbiology2008
Characterization of the pattern of alphas1- and beta-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 87 citations in OpenAlex.
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- In Silico Comparative Genomic Analysis Revealed a Highly Conserved Proteolytic System inInternational journal of molecular sciences · 2023Article
- Valorization of leftover green tea residues through conversion to bioactive peptides using probiotics-aided anaerobic digestion.Microbial biotechnology · 2023Article
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- Angiotensin-I-Converting Enzyme Inhibitory Peptides in Goat Milk Fermented by Lactic Acid Bacteria Isolated from Fermented Food and Breast Milk.Food science of animal resources · 2022Article
- Effects of Protein, Calcium, and pH on Gene Transcription, Cell-Envelope Peptidase Activity ofFoods (Basel, Switzerland) · 2021Article
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- Use of Mass Spectrometry to Profile Peptides in Whey Protein Isolate Medium Fermented byFrontiers in nutrition · 2019Article
- Mechanistic Insights Into Probiotic Properties of Lactic Acid Bacteria Associated With Ethnic Fermented Dairy Products.Frontiers in microbiology · 2019Review
- Diversity and Functional Properties of Lactic Acid Bacteria Isolated From Wild Fruits and Flowers Present in Northern Argentina.Frontiers in microbiology · 2019Article
- Production of Bioactive Peptides byFrontiers in microbiology · 2018Review
- YebC, a putative transcriptional factor involved in the regulation of the proteolytic system of Lactobacillus.Scientific reports · 2017Article
- Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines.Frontiers in microbiology · 2016Review
- Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563.Korean journal for food science of animal resources · 2015Article
- Genome Sequence of the Cheese-Starter Strain Lactobacillus delbrueckii subsp. lactis CRL 581.Genome announcements · 2013Article
- Simultaneous presence of PrtH and PrtH2 proteinases in Lactobacillus helveticus Strains improves breakdown of the pure alphas1-casein.Applied and environmental microbiology · 2011Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEP(I/III) variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the alpha(s1)- and beta-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of alpha(s1)- and beta-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized.
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