scholarly journals Effects of heat treatment of cow's milk and whey on the nutritional quality and antigenic properties.

1982 ◽  
Vol 57 (11) ◽  
pp. 842-847 ◽  
Author(s):  
P J Kilshaw ◽  
L M Heppell ◽  
J E Ford
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.


1959 ◽  
Vol 68 (2) ◽  
pp. 265-279 ◽  
Author(s):  
R. M. Tomarelli ◽  
Nancy Minnick ◽  
Elisa D'amato ◽  
F. W. Bernhart

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

2008 ◽  
Vol 71 (6) ◽  
pp. 1270-1272 ◽  
Author(s):  
H. KADDOURI ◽  
S. MIMOUN ◽  
K. E. EL-MECHERFI ◽  
A. CHEKROUN ◽  
O. KHEROUA ◽  
...  

This study evaluated the effects of γ-radiation on the antigenic properties of β-lactoglobulin in cow's milk. Liquid and lyophilized samples of cow's milk and whey were irradiated with γ-cells (60Co) at dose levels of 3, 5, and 10 kGy, at room temperature in the presence of air. Effects of treatment on proteins were monitored by Lowry's method, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, and enzyme-linked immunosorbent assay. Radiation did not affect the molecular-weight distributions of proteins, but it did reduce their solubility. Furthermore, results showed that irradiation at 10 kGy increased the recognition of milk and whey powders by anti–β-lactoglobulin (β-Lg) rabbit immunoglobulin G, with the other samples remaining antigenically stable. These results indicate that γ-rays do not reduce cow's milk β-lactoglobulin antigenicity.


1998 ◽  
Vol 62 (1) ◽  
pp. 21-25 ◽  
Author(s):  
L.H. Foster ◽  
M.F. Chaplin ◽  
S. Sumar

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

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