חיפוש מתקדם
International Dairy Journal
Fleminger, G., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Ragones, H., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Merin, U., Department of Food Science, Institute of Technology and Storage of Agricultural Products, A.R.O, The Volcani Center, P.O. Box. 6, Bet Dagan 50250, Israel
Silanikove, N., Biology of Lactation Laboratory, Institute of Animal Science, A.R.O, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Leitner, G., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Previously it was shown that a low molecular mass fraction isolated from the proteose-peptone preparation of milk, fraction E, inhibited milk coagulation. Here, the composition and molecular mass of fraction E, and its effect on milk clotting parameters, was investigated to better understand its mechanism of action. Fraction E comprised casein-derived peptides of 1-3 kDa rich in phosphorus residues. Fraction E content increased substantially in milk from glands infected with Escherichia coli and Streptococcus dysgalactiae, and during storage of the milk. However, the specific activity of fraction E on milk clotting parameters was the same whether sampled from healthy, infected or stored milk. The inhibitory effect was reversible on adding 0.75 mm CaCl2, suggesting that chelation of Ca by fraction E was involved in the inhibitory mechanism. However, only partial recovery was achieved and an excess of Ca was required, suggesting the involvement of additional pathways in the process. © 2013 Elsevier Ltd.
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הספר "אוצר וולקני"
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תנאי שימוש
Low molecular mass peptides generated by hydrolysis of casein impair rennet coagulation of milk
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Fleminger, G., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Ragones, H., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Merin, U., Department of Food Science, Institute of Technology and Storage of Agricultural Products, A.R.O, The Volcani Center, P.O. Box. 6, Bet Dagan 50250, Israel
Silanikove, N., Biology of Lactation Laboratory, Institute of Animal Science, A.R.O, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Leitner, G., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Low molecular mass peptides generated by hydrolysis of casein impair rennet coagulation of milk
Previously it was shown that a low molecular mass fraction isolated from the proteose-peptone preparation of milk, fraction E, inhibited milk coagulation. Here, the composition and molecular mass of fraction E, and its effect on milk clotting parameters, was investigated to better understand its mechanism of action. Fraction E comprised casein-derived peptides of 1-3 kDa rich in phosphorus residues. Fraction E content increased substantially in milk from glands infected with Escherichia coli and Streptococcus dysgalactiae, and during storage of the milk. However, the specific activity of fraction E on milk clotting parameters was the same whether sampled from healthy, infected or stored milk. The inhibitory effect was reversible on adding 0.75 mm CaCl2, suggesting that chelation of Ca by fraction E was involved in the inhibitory mechanism. However, only partial recovery was achieved and an excess of Ca was required, suggesting the involvement of additional pathways in the process. © 2013 Elsevier Ltd.
Scientific Publication
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