The effect of heat treatment on intrinsic and fortified selenium levels in cow's milk

1998 ◽  
Vol 62 (1) ◽  
pp. 21-25 ◽  
Author(s):  
L.H. Foster ◽  
M.F. Chaplin ◽  
S. Sumar
Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1836
Author(s):  
Hannah E. Zenker ◽  
Malgorzata Teodorowicz ◽  
Harry J. Wichers ◽  
Kasper A. Hettinga

For the determination of the binding of heated cow’s milk whey proteins such as β-lactoglobulin to the receptors expressed on immune cells, inhibition ELISA with the soluble form of the receptor for advanced glycation end products (sRAGE) and scavenger receptor class B (CD36) has been successfully used in the past. However, binding to heated and glycated caseins in this read-out system has not been tested. In this study, inhibition ELISA was applied to measure the binding of cow’s milk casein alone, as well as all milk proteins together, which underwent differential heat treatment, to sRAGE and CD36, and we compared those results to a dot blot read out. Moreover, binding to sRAGE and CD36 of differentially heated milk protein was measured before and after in vitro digestion. Casein showed binding to sRAGE and CD36, independent from the heat treatment, in ELISA, while the dot blot showed only binding to high-temperature-heated milk protein, indicating that the binding is not related to processing but to the physicochemical characteristics of the casein. This binding decreased after passage of casein through the intestinal phase.


1970 ◽  
Vol 37 (3) ◽  
pp. 397-405 ◽  
Author(s):  
E. J. Hindle ◽  
J. V. Wheelock

SummaryThe release, as a result of heat treatment on cow's milk, of peptides and glycopeptides which are soluble in the 12% trichloroacetic acid (TCA) filtrate of the milk has been studied. The results showed that the amount of peptides released increased with temperature and duration of the heat treatment. There were differences between milks in their response to a given heat treatment. Glycopeptides were released at temperatures as low as 50 °C but not at 37 °C. A comparison was made of the glycopeptides released by heat treatment and of those released from κ-casein by the action of rennin on the milk. This showed that N-acetyl neuraminic acid, D-galactose and 2-acetamido-2-deoxy-D-galactose were invariably present in both groups of glycopeptides. D-Mannose was also present in the glycopeptides released by heat but was detected on the glycopeptides released by rennin in only one of 6 experiments. It is suggested that glycopeptides released by heat may be derived from κ-casein but that a definite conclusion cannot be reached at present because of lack of information on the carbohydrates attached to other milk proteins.


2014 ◽  
Vol 2 (4) ◽  
pp. 259 ◽  
Author(s):  
Hee Seon Lee ◽  
Mi Na Kim ◽  
Jung Yeon Hong ◽  
Won Il Heo ◽  
Kyung Won Kim ◽  
...  

2009 ◽  
Vol 39 (6) ◽  
pp. 918-925 ◽  
Author(s):  
Y. Morisawa ◽  
A. Kitamura ◽  
T. Ujihara ◽  
N. Zushi ◽  
K. Kuzume ◽  
...  

2020 ◽  
Vol 11 (6) ◽  
pp. 4982-4993 ◽  
Author(s):  
Suzanne Abbring ◽  
Ling Xiong ◽  
Mara A. P. Diks ◽  
Ton Baars ◽  
Johan Garssen ◽  
...  

Whey proteins denaturing ≤65 °C are important for allergy protection by raw cow's milk.


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