Peptides from several italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, pseudomonas fluorescens ATCC 948 and to the angiotensin I-converting enzyme
| Autor: | E. Smacchi, Marco Gobbetti |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Streptococcus thermophilus
Lactobacillus casei biology Lactococcus lactis Proteolytic enzymes food and beverages Bioengineering Pseudomonas fluorescens biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Endopeptidase Lactic acid chemistry.chemical_compound chemistry Lactobacillus Biotechnology |
| Zdroj: | Enzyme and Microbial Technology. 22:687-694 |
| ISSN: | 0141-0229 |
| DOI: | 10.1016/s0141-0229(97)00261-5 |
| Popis: | Water-soluble peptides from Mozzarella, Italico, Crescenza, and Gorgonzola cheeses were fractionated by reverse-phase fast protein liquid chromatography. Peptide fractions with inhibitory activity to amino- and endo-peptidases from Lactobacillus delbrueckii ssp. bulgaricus B397, Streptococcus thermophilus 305, and Lactococcus lactis ssp. cremoris Wg2 were found. Enzymes from Lactobacillus casei ssp. casei 2752 were less sensitive. Endopeptidase from Lactobacillus casei ssp. casei 2752 also had a different response to the effect of some inhibitors. It probably showed limited differences in catalysis and substrate positioning. Most of these inhibitory peptides were also effective in reducing the activity of the Pseudomonas fluorescens ATCC 948 endopeptidase and the angiotensin I-converting enzyme. Inhibitory peptide fractions from Mozzarella, Italico, and Crescenza cheeses had a certain degree of hydrophobicity while the peptide fraction from Gorgonzola cheese eluted in the initial part of the acetonitrile gradient. One of the inhibitory peptides contained in the water-soluble extract of Crescenza cheese was further purified and sequenced. It corresponded to the β-casein fragment 58-72. |
| Databáze: | OpenAIRE |
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