INLAIN   20354
INSTITUTO DE LACTOLOGIA INDUSTRIAL
Unidad Ejecutora - UE
artículos
Título:
Production of peptides and free amino acids in a sterile extract describes peptidolysis in hard-cooked cheeses
Autor/es:
MILESI, MARÍA M.; BERGAMINI, CARINA V.; HYNES, ERICA R.
Revista:
FOOD RESEARCH INTERNATIONAL
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2011 vol. 44 p. 765 - 773
ISSN:
0963-9969
Resumen:
Hard cooked cheeses are mostly manufactured with lactic starters of Lactobacillus helveticus, which constitute
a major proteolytic agent in the food. In this work, we assessed the proteolysis produced by enzymes of two
strains of L. helveticus in a new cheese model, which consisted of a sterile substrate prepared with hardcooked
cheeses, and identified the time of ripening when main changes in proteolysis are produced. The
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheeses, and identified the time of ripening when main changes in proteolysis are produced. The
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble
peptides and free amino acids. Great variation in peptide profiles was found as incubation progressed in
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
cheese extracts, which evidenced that proteases and peptidases from the starter were active and able to
degrade the proteinaceous material available in the extracts. The extracts derived from cheeses with
extract, a representative model of the aqueous phase of the cheeses, was obtained from Reggianito cheeses of
different ripening times (3, 90, and 180 days) made with starters composed of the strains tested, either SF138
or SF209. To obtain the substrate, the cheese was extracted with water, then centrifuged and the aqueous
phase was sterilized by filtration through membrane (0.45 ìm). The substrates were incubated at 34 °C during
21 days; samples were taken at 0, 3, 7, 14, and 21 days. Sterility was verified by plating samples on skim milk
agar and incubating at 37 °C for 48 h. Proteolysis was determined by liquid chromatography of soluble