Further evidence in the case against heated milk protein

1972 ◽  
Vol 15 (1) ◽  
pp. 129-133 ◽  
Author(s):  
J ANNAND
Keyword(s):  
Milk Protein ◽  
Heated Milk

Effects of β-lactoglobulin and κ-casein genetic variants and concentrations on syneresis of gels from renneted heated milk

1989 ◽  
Vol 56 (2) ◽  
pp. 297-301 ◽  
Author(s):  
Douglas M. McLean ◽  
Johan Schaar
Keyword(s):  
Genetic Polymorphism ◽  
Complex Formation ◽  
Genetic Variants ◽  
Milk Protein ◽  
Major Influence ◽  
Essential Requirement ◽  
Heated Milk ◽  
Cheese Curd ◽  
Processing Properties ◽  
Β Lactoglobulin

Milk protein genetic polymorphism has a major influence on the composition of milk, and on its processing properties, including yield of cheese (see Schaaret al.1985; McLeanet al.1984, 1987; McLean, 1987). However, there appears to be little information on the effects of milk protein genetic variants on syneresis of cheese curd. The effect of casein composition on syneresis was studied by Pearseet al.(1986), who found that syneresis was affected only by the level of β-casein. Syneresis is an essential requirement in cheese making from renneted or acidified milk, but is undesirable during the storage of products such as yogurt. Milk for yogurt manufacture is preheated to minimize syneresis and to give maximal firmness of the yogurt coagulum (Tamime & Deeth, 1980). Pearseet al.(1985) showed that the reduction of one-third in the extent of syneresis caused by heating artificial micelle milk (AMM) containing βlactoglobulin (β-lg) in natural concentrations was due to sulphydryl-mediated complex formation between β-lg and micellar κ-casein which appeared to interfere with the micelle–micelle interactions responsible for syneresis. The results presented here were part of a study which investigated the effects of κcasein and κ-lg genetic variants and concentrations on syneresis of curd formed from renneted heated AMM.

Use of heated milk protein–sugar blends as antioxidant in dairy beverages enriched with linseed oil

LWT ◽  
2010 ◽  
Vol 43 (9) ◽  
pp. 1373-1378 ◽  
Author(s):  
Hélène J. Giroux ◽  
Jessica Houde ◽  
Michel Britten
Keyword(s):  
Milk Protein ◽  
Linseed Oil ◽  
Heated Milk ◽  
Dairy Beverages

scholarly journals No Glycation Required: Interference of Casein in AGE Receptor Binding Tests

Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1836
Author(s):  
Hannah E. Zenker ◽  
Malgorzata Teodorowicz ◽  
Harry J. Wichers ◽  
Kasper A. Hettinga
Keyword(s):  
Heat Treatment ◽  
Milk Protein ◽  
Soluble Form ◽  
Cow’S Milk ◽  
Dot Blot ◽  
Differential Heat ◽  
Cow's Milk ◽  
Inhibition Elisa ◽  
Heated Milk

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.

Effect of the protein, citrate and phosphate content of milk on formation of lactulose during heat treatment

1987 ◽  
Vol 54 (2) ◽  
pp. 207-218 ◽  
Author(s):  
Geoffrey R. Andrews ◽  
S. Krishna Prasad
Keyword(s):  
Heat Treatment ◽  
Milk Protein ◽  
Buffering Capacity ◽  
Phosphate Content ◽  
Mechanism Of Formation ◽  
Amino Groups ◽  
Base Catalysts ◽  
Naturally Occurring ◽  
Heated Milk ◽  
Skimmed Milk

SummaryMilk ultrafiltrate and milks of varying protein, citrate and phosphate concentrations were heated in sealed containers. Protein was found not to be involved in the mechanism of formation of lactulose, but increasing the protein content of milk reduced the concentration of lactulose after heating. This was considered to be due to increased condensation of lactose and lactulose with amino groups of the protein, Less lactulose was formed in milk ultrafiltrate than in skimmed milk accorded the same heat treatment, which was attributed to the buffering capacity of the milk protein in skimmed milk. Activation energies for lactulose formation in skimmed milk and in ultrafiltrate were 128 and 131 kJ/mol respectively. Citrate and phosphate catalysed the formation of lactulose. It is proposed that the formation of free lactulose in heated milk and ultrafiltrate proceeds exclusively by the Lobry de Bruyn-Alberda van Ekenstein transformation with the naturally occurring phosphate and citrate acting as base catalysts.

Antibodies to heated milk protein in coronary heart disease

1980 ◽  
Vol 37 (1) ◽  
pp. 151-155 ◽  
Author(s):  
Michael J. Gibney ◽  
Patrick J. Gallagher ◽  
Geoffrey P. Sharratt ◽  
Harjit S. Benning ◽  
T. Geoffrey Taylor ◽  
...  
Keyword(s):  
Coronary Heart Disease ◽  
Heart Disease ◽  
Milk Protein ◽  
Heated Milk

29. The Effect of Heat upon the Rennin Coagulation. II

1931 ◽  
Vol 3 (1-2) ◽  
pp. 80-85 ◽  
Author(s):  
George M. Moir
Keyword(s):  
Lactic Acid ◽  
Soluble Protein ◽  
Milk Protein ◽  
Starter Culture ◽  
Raw Milk ◽  
Experimental Results ◽  
Coagulation Time ◽  
Casein Micelles ◽  
Heated Milk

1. Clean milk has been “flash” pasteurised at 165°F. Portions of the same raw milk have been treated with small amounts respectively of starter culture and lactic acid, so as to raise the acidity, before being similarly pasteurised.2. Comparison of the whey obtained by rennetting the three raw portions has shown that those from the acidified milk contained more soluble protein than the original.3. The differences between the raw and pasteurised milk in their coagulation time with rennin have been found to be proportionately much greater in the acidified portions.4. These differences in coagulation time have been shown to be correlated with decreases in the amount of soluble protein found in. the whey separated from the coagulum.5. These experimental results, together with those of other investigators, have been made the basis of a suggestion that the decreased coagulability of heated milk with rennin is partly due to flocculation of soluble milk protein upon the casein micelles.

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