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פותח על ידי קלירמאש פתרונות בע"מ -
Chemical and structural characterization of bacterially-derived casein peptides that impair milk clotting
Year:
2011
Source of publication :
International Dairy Journal
Authors :
מרין, עוזי
;
.
סילניקוב, ניסים
;
.
Volume :
21
Co-Authors:
Fleminger, G., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Heftsi, R., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Uzi, M., 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
Nissim, S., Biology of Lactation Laboratory, Institute of Animal Science, A.R.O., The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Gabriel, L., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Facilitators :
From page:
914
To page:
920
(
Total pages:
7
)
Abstract:
Milk-clotting parameters are highly affected by hydrolysis of casein. Previously, it was shown that products of the hydrolysis of casein impair milk clotting, affecting both clotting time and curd firmness. One of these fractions is of particular interest since it is produced exclusively by enzymes of Streptococcus dysgalactiae. The present study aims to further investigate the chemical and structural properties of this fraction in an attempt to understand its influence on milk clotting. Preparations of this fraction, obtained from either S. dysgalactiae-infected glands or ex vivo inoculations with the same bacteria, were found to be identical. Mass spectrometry and Edman degradation analyses indicate that it comprises primarily β-CN83-209, generated by cleavage at a Val-Val peptide bond, presumably by bacterial thermolysin- or elastin-like proteases. A model offering a putative mechanism for interference with milk-clotting parameters through production of this fraction is presented. © 2011 Elsevier Ltd.
Note:
Related Files :
casein
Clotting time
Edman degradation
Hydrolysis
Peptide bonds
peptides
Streptococcus dysgalactiae
thermolysin
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.idairyj.2011.05.012
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
24303
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:06
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Scientific Publication
Chemical and structural characterization of bacterially-derived casein peptides that impair milk clotting
21
Fleminger, G., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Heftsi, R., Department of Molecular Microbiology and Biotechnology, The George Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv 69978, Israel
Uzi, M., 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
Nissim, S., Biology of Lactation Laboratory, Institute of Animal Science, A.R.O., The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Gabriel, L., National Mastitis Reference Center, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel
Chemical and structural characterization of bacterially-derived casein peptides that impair milk clotting
Milk-clotting parameters are highly affected by hydrolysis of casein. Previously, it was shown that products of the hydrolysis of casein impair milk clotting, affecting both clotting time and curd firmness. One of these fractions is of particular interest since it is produced exclusively by enzymes of Streptococcus dysgalactiae. The present study aims to further investigate the chemical and structural properties of this fraction in an attempt to understand its influence on milk clotting. Preparations of this fraction, obtained from either S. dysgalactiae-infected glands or ex vivo inoculations with the same bacteria, were found to be identical. Mass spectrometry and Edman degradation analyses indicate that it comprises primarily β-CN83-209, generated by cleavage at a Val-Val peptide bond, presumably by bacterial thermolysin- or elastin-like proteases. A model offering a putative mechanism for interference with milk-clotting parameters through production of this fraction is presented. © 2011 Elsevier Ltd.
Scientific Publication
You may also be interested in