Water-solubleextracts of 9 Italiancheesevarieties that differed mainly for type of cheese milk, starter, technology, and time of ripening were fractionated by reversed-phase fast protein liquid chromatography, and the antimicrobial activity of each fraction was first assayed toward Lactobacillus sakei A15 by well-diffusion assay. Active fractions were further analyzed by HPLC coupled to electrospray ionization-ion trap mass spectrometry, and peptide sequences were identified by comparison with a proteomic database. Parmigiano Reggiano, Fossa, and Gorgonzola water-solubleextracts did not show antibacterialpeptides. Fractions of Pecorino Romano, Canestrato Pugliese, Crescenza, and Caprino del Piemonte contained a mixture of peptides with a high degree of homology. Pasta filata cheeses (Caciocavallo and Mozzarella) also had antibacterialpeptides. Peptides showed high levels of homology with N-terminal, C-terminal, or whole fragments of well known antimicrobial or multifunctional peptides reported in the literature: αS1-casokinin (e.g., sheep αS1-casein (CN) f22–30 of Pecorino Romano and cow αS1-CN f24–33 of Canestrato Pugliese); isracidin (e.g., sheep αS1-CN f10–21 of Pecorino Romano); kappacin and casoplatelin (e.g., cow κ-CN f106–115 of Canestrato Pugliese and Crescenza); and β-casomorphin-11 (e.g., goat β-CN f60–68 of Caprino del Piemonte). As shown by the broth microdilution technique, most of the water-soluble fractions had a large spectrum of inhibition (minimal inhibitory concentration of 20 to 200 μg/mL) toward gram-positive and gram-negative bacterial species, including potentially pathogenic bacteria of clinical interest. Cheeses manufactured from different types of cheese milk (cow, sheep, and goat) have the potential to generate similar peptides with antimicrobial activity.

Water-soluble extracts of 9 Italian cheese varieties that differed mainly for type of cheese milk, starter, technology, and time of ripening were fractionated by reversed-phase fast protein liquid chromatography, and the antimicrobial activity of each fraction was first assayed toward Lactobacillus sakei A15 by well-diffusion assay. Active fractions were further analyzed by HPLC coupled to electrospray ionization-ion trap mass spectrometry, and peptide sequences were identified by comparison with a proteomic database. Parmigiano Reggiano, Fossa, and Gorgonzola water-soluble extracts did not show antibacterial peptides. Fractions of Pecorino Romano, Canestrato Pugliese, Crescenza, and Caprino del Piemonte contained a mixture of peptides with a high degree of homology. Pasta filata cheeses (Caciocavallo and Mozzarella) also had antibacterial peptides. Peptides showed high levels of homology with N-terminal, C-terminal, or whole fragments of well known antimicrobial or multifunctional peptides reported in the literature: αS1-casokinin (e.g., sheep αS1- casein (CN) f22–30 of Pecorino Romano and cow αS1- CN f24–33 of Canestrato Pugliese); isracidin (e.g., sheep αS1-CN f10–21 of Pecorino Romano); kappacin and casoplatelin (e.g., cow κ-CN f106–115 of Canestrato Pugliese and Crescenza); and β-casomorphin-11 (e.g., goat β-CN f60–68 of Caprino del Piemonte). As shown by the broth microdilution technique, most of the watersoluble fractions had a large spectrum of inhibition (minimal inhibitory concentration of 20 to 200 μg/mL) toward gram-positive and gram-negative bacterial species, including potentially pathogenic bacteria of clinical interest. Cheeses manufactured from different types of cheese milk (cow, sheep, and goat) have the potential to generate similar peptides with antimicrobial activity.

Antibacterial activities of peptides from the water-soluble extracts of Italian cheese varieties / Rizzello, Cg; Losito, I; Gobbetti, M; Carbonara, T; De Bari, Md; Zambonin, Pg. - In: JOURNAL OF DAIRY SCIENCE. - ISSN 1525-3198. - 88:(2005), pp. 2348-2360.

Antibacterial activities of peptides from the water-soluble extracts of Italian cheese varieties

RIZZELLO CG;
2005

Abstract

Water-soluble extracts of 9 Italian cheese varieties that differed mainly for type of cheese milk, starter, technology, and time of ripening were fractionated by reversed-phase fast protein liquid chromatography, and the antimicrobial activity of each fraction was first assayed toward Lactobacillus sakei A15 by well-diffusion assay. Active fractions were further analyzed by HPLC coupled to electrospray ionization-ion trap mass spectrometry, and peptide sequences were identified by comparison with a proteomic database. Parmigiano Reggiano, Fossa, and Gorgonzola water-soluble extracts did not show antibacterial peptides. Fractions of Pecorino Romano, Canestrato Pugliese, Crescenza, and Caprino del Piemonte contained a mixture of peptides with a high degree of homology. Pasta filata cheeses (Caciocavallo and Mozzarella) also had antibacterial peptides. Peptides showed high levels of homology with N-terminal, C-terminal, or whole fragments of well known antimicrobial or multifunctional peptides reported in the literature: αS1-casokinin (e.g., sheep αS1- casein (CN) f22–30 of Pecorino Romano and cow αS1- CN f24–33 of Canestrato Pugliese); isracidin (e.g., sheep αS1-CN f10–21 of Pecorino Romano); kappacin and casoplatelin (e.g., cow κ-CN f106–115 of Canestrato Pugliese and Crescenza); and β-casomorphin-11 (e.g., goat β-CN f60–68 of Caprino del Piemonte). As shown by the broth microdilution technique, most of the watersoluble fractions had a large spectrum of inhibition (minimal inhibitory concentration of 20 to 200 μg/mL) toward gram-positive and gram-negative bacterial species, including potentially pathogenic bacteria of clinical interest. Cheeses manufactured from different types of cheese milk (cow, sheep, and goat) have the potential to generate similar peptides with antimicrobial activity.
2005
Water-solubleextracts of 9 Italiancheesevarieties that differed mainly for type of cheese milk, starter, technology, and time of ripening were fractionated by reversed-phase fast protein liquid chromatography, and the antimicrobial activity of each fraction was first assayed toward Lactobacillus sakei A15 by well-diffusion assay. Active fractions were further analyzed by HPLC coupled to electrospray ionization-ion trap mass spectrometry, and peptide sequences were identified by comparison with a proteomic database. Parmigiano Reggiano, Fossa, and Gorgonzola water-solubleextracts did not show antibacterialpeptides. Fractions of Pecorino Romano, Canestrato Pugliese, Crescenza, and Caprino del Piemonte contained a mixture of peptides with a high degree of homology. Pasta filata cheeses (Caciocavallo and Mozzarella) also had antibacterialpeptides. Peptides showed high levels of homology with N-terminal, C-terminal, or whole fragments of well known antimicrobial or multifunctional peptides reported in the literature: αS1-casokinin (e.g., sheep αS1-casein (CN) f22–30 of Pecorino Romano and cow αS1-CN f24–33 of Canestrato Pugliese); isracidin (e.g., sheep αS1-CN f10–21 of Pecorino Romano); kappacin and casoplatelin (e.g., cow κ-CN f106–115 of Canestrato Pugliese and Crescenza); and β-casomorphin-11 (e.g., goat β-CN f60–68 of Caprino del Piemonte). As shown by the broth microdilution technique, most of the water-soluble fractions had a large spectrum of inhibition (minimal inhibitory concentration of 20 to 200 μg/mL) toward gram-positive and gram-negative bacterial species, including potentially pathogenic bacteria of clinical interest. Cheeses manufactured from different types of cheese milk (cow, sheep, and goat) have the potential to generate similar peptides with antimicrobial activity.
antibacterial peptides; cheeses; lactic acid bacteria
01 Pubblicazione su rivista::01a Articolo in rivista
Antibacterial activities of peptides from the water-soluble extracts of Italian cheese varieties / Rizzello, Cg; Losito, I; Gobbetti, M; Carbonara, T; De Bari, Md; Zambonin, Pg. - In: JOURNAL OF DAIRY SCIENCE. - ISSN 1525-3198. - 88:(2005), pp. 2348-2360.
File allegati a questo prodotto
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1459168
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 176
  • ???jsp.display-item.citation.isi??? 138
social impact