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{Hebert2008CharacterizationOT,
  title={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.},
  author={Elvira Maria Hebert and Gianfranco Mamone and Gianluca Picariello and Ra{\'u}l Ricardo Raya and Graciela Savoy and Pasquale Ferranti and Francesco Addeo},
  journal={Applied and environmental microbiology},
  year={2008},
  volume={74 12},
  pages={3682-9}
}
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… CONTINUE READING

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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 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 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 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 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 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 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 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 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 .
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