Disorder in Milk Proteins: Formation, Structure, Function, Isolation and Applications of Casein Phosphopeptides

2016 ◽  
Vol 17 (4) ◽  
pp. 368-379 ◽  
Author(s):  
Muhammad Ali Naqvi ◽  
Kimia Anaraki Irani ◽  
Maryam Katanishooshtari ◽  
Dérick Rousseau
2001 ◽  
Vol 12 (9) ◽  
pp. 339-346 ◽  
Author(s):  
P.X Qi ◽  
E.M Brown ◽  
H.M Farrell

2000 ◽  
Vol 84 (S1) ◽  
pp. 3-10 ◽  
Author(s):  
Nagendra P. Shah

Milk contains various components with physiological functionality. Peptides derived from caseins and whey proteins including opioid peptides, antihypertensive peptides, casein phosphopeptides, α- and β-lactorphins and albutensin have been shown to possess various bioactive properties. This review considers an overview of the bioactive components in milk proteins and whey and their physiological function.


2002 ◽  
Vol 85 (3) ◽  
pp. 459-471 ◽  
Author(s):  
H.M. Farrell ◽  
P.X. Qi ◽  
E.M. Brown ◽  
P.H. Cooke ◽  
M.H. Tunick ◽  
...  

Author(s):  
Robert J. Carroll ◽  
Marvin P. Thompson ◽  
Harold M. Farrell

Milk is an unusually stable colloidal system; the stability of this system is due primarily to the formation of micelles by the major milk proteins, the caseins. Numerous models for the structure of casein micelles have been proposed; these models have been formulated on the basis of in vitro studies. Synthetic casein micelles (i.e., those formed by mixing the purified αsl- and k-caseins with Ca2+ in appropriate ratios) are dissimilar to those from freshly-drawn milks in (i) size distribution, (ii) ratio of Ca/P, and (iii) solvation (g. water/g. protein). Evidently, in vivo organization of the caseins into the micellar form occurs in-a manner which is not identical to the in vitro mode of formation.


Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
J Usta ◽  
K Racha ◽  
K Boushra ◽  
S Shatha ◽  
B Yolla ◽  
...  

1993 ◽  
Vol 70 (01) ◽  
pp. 177-179 ◽  
Author(s):  
Daniel B Rifkin ◽  
Soichi Kojima ◽  
Mayumi Abe ◽  
John G Harpel
Keyword(s):  

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