scholarly journals Fractionation of the Two Major Whey Proteins in an Electrophoretic Membrane Contactor

2012 ◽  
Vol 44 ◽  
pp. 830-832
Author(s):  
S. Galier ◽  
H. Roux-de Balmann
2018 ◽  
pp. 49-51
Author(s):  
E.B. Stanislavskaya ◽  
◽  
E.I. Melnikova ◽  
Keyword(s):  

2019 ◽  
Vol 56 (6) ◽  
pp. 54-56
Author(s):  
E.Yu. Agarkova ◽  
◽  
A.G. Kruchinin ◽  
A.A. Agarkov ◽  
V.D. Haritonov

1983 ◽  
Vol 50 (3) ◽  
pp. 275-290 ◽  
Author(s):  
Anthony T. Andrews ◽  
Efstathios Alichanidis

SummaryThe proteolysis of highly purified samples of αs1-, αs2-, β-and κ-caseins by porcine plasmin and by bovine plasminogen with urokinase has been examined principally by gel electrophoresis. The resulting peptide band patterns were compared with those of total proteose-peptone (TPP) samples prepared from fresh and stored raw and pasteurized milk, and also with those obtained during the natural course of proteolysis by indigenous enzymes in milk during storage. TPP was found to contain at least 38 components detectable by a single electrophoresis run. Apart from residual traces of whey proteins and intact caseins nearly all of these components were fragments of caseins produced by indigenous plasmin, with products from the breakdown of αs1- and β-casein predominating. Over 90 % of TPP has been accounted for in this way. A fragment consisting of residues 29–105 of β-casein was isolated and characterized from both stored milk and from plasmin digests of β-casein. This fragment was a relatively major product of the natural proteolysis occurring during storage of milk, but contrary to a report in the literature it was not the same as proteose-peptone component 8-slow. Since many of the components of TPP resulted from proteolysis, the composition of TPP was found to vary according to the time and temperature of storage of the milk from which it was prepared. Thus, while the proteose-peptone fraction of milk can easily be defined operationally it cannot be rigorously defined in terms of its composition unless the history of the milk is also defined.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
P. K. Rout ◽  
M. Verma

AbstractGoat milk is a source of nutrition in difficult areas and has lesser allerginicity than cow milk. It is leading in the area for nutraceutical formulation and drug development using goat mammary gland as a bioreactor. Post translational modifications of a protein regulate protein function, biological activity, stabilization and interactions. The protein variants of goat milk from 10 breeds were studied for the post translational modifications by combining highly sensitive 2DE and Q-Exactive LC-MS/MS. Here we observed high levels of post translational modifications in 201 peptides of 120 goat milk proteins. The phosphosites observed for CSN2, CSN1S1, CSN1S2, CSN3 were 11P, 13P, 17P and 6P, respectively in 105 casein phosphopeptides. Whey proteins BLG and LALBA showed 19 and 4 phosphosites respectively. Post translational modification was observed in 45 low abundant non-casein milk proteins mainly associated with signal transduction, immune system, developmental biology and metabolism pathways. Pasp is reported for the first time in 47 sites. The rare conserved peptide sequence of (SSSEE) was observed in αS1 and αS2 casein. The functional roles of identified phosphopeptides included anti-microbial, DPP-IV inhibitory, anti-inflammatory and ACE inhibitory. This is first report from tropics, investigating post translational modifications in casein and non-casein goat milk proteins and studies their interactions.


2021 ◽  
Vol 627 ◽  
pp. 119232
Author(s):  
Mei Li ◽  
Zhihao Zhu ◽  
Meiqing Zhou ◽  
Xingming Jie ◽  
Lina Wang ◽  
...  

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