Effect of pH on Heat Stability in Skim Milk Subjected to Demineralization by Means of Electrodialysis with Ion Permselective Membrane

1977 ◽  
Vol 48 (9) ◽  
pp. 437-438
Author(s):  
Shigeo OKONOGI ◽  
Mamoru TOMITA
2021 ◽  
pp. 106757
Author(s):  
Jianfeng Wu ◽  
Simin Chen ◽  
Teng Wang ◽  
Hao Li ◽  
Ali Sedaghat Doost ◽  
...  

2004 ◽  
Vol 14 (5) ◽  
pp. 437-443 ◽  
Author(s):  
C. Guillaume ◽  
E. Gastaldi ◽  
J.-L. Cuq ◽  
S. Marchesseau
Keyword(s):  

1980 ◽  
Vol 47 (3) ◽  
pp. 327-335 ◽  
Author(s):  
A. W. Maurice Sweetsur ◽  
D. Donald Muir

SUMMARYAn examination has been made of the heat stability characteristics of skim-milk concentrate prepared by ultrafiltration (UF). Concentrate prepared by UF was found to be more stable than that prepared by conventional evaporation. In contrast to conventional concentrate, the heat stability of UF concentrate was not appreciably affected by forewarming or addition of permitted stabilizers, but the effect of addition of urea was generally the same for both UF and conventional concentrates; an increase in heat stability was obtained if the milk total solids level was less than 14%. As with conventional concentrate, addition of simple aldehydes induced large increases in the heat stability of UF concentrate. It is suggested that a novel range of sterile milk products could be prepared from UF concentrates. Because of the high protein and low lactose contents of these concentrates, the products might be nutritionally more attractive than those prepared from conventional concentrates.


2018 ◽  
Vol 71 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Joseph Dumpler ◽  
Felicitas Peraus ◽  
Verena Depping ◽  
Bryndís Stefánsdóttir ◽  
Martin Grunow ◽  
...  

1979 ◽  
Vol 46 (2) ◽  
pp. 401-405 ◽  
Author(s):  
Nripendra C. Ganguli

SUMMARYBuffalo skim-milk is less heat stable than cow skim-milk. Interchanging ultracentrifugal whey (UCW) and milk diffusate with micellar casein caused significant changes in the heat stability of buffalo casein micelles (BCM) and cow casein micelles (CCM). Buffalo UCW dramatically destabilized COM, whereas buffalo diffu-sate with CCM exhibited the highest heat stability.Cow κ-casein stabilizes αs-casein against precipitation by Ca better than buffalo º-casein. About 90% of αs-casein could be stabilized by κ: αs ratios of 0·20 and 0·231 for cow and buffalo, respectively.Sialic acid release from micellar κ-casein by rennet was higher than from acid κ-casein in both buffalo and cow caseins, the release being slower in buffalo. The released macropeptide from buffalo κ-casein was smaller than that from cow κ-casein as revealed by Sephadex gel filtration.Sub-units of BCM have less sialic acid (1·57mg/g) than whole micelles (2·70mg/g). On rennet action, 47% of bound sialic acid was released from sub-units as against 85% from whole micelles. The sub-micelles are less heat stable than whole micelles. Among ions tested, added Ca reduced heat stability more dramatically in whole micelles, whereas added phosphate improved the stability of micelles and, more strikingly, of sub-micelles. Citrate also improved the heat stability of sub-micelles but not of whole micelles.


2014 ◽  
Vol 35 (1) ◽  
pp. 102-105 ◽  
Author(s):  
Qiming Li ◽  
Ying Ma ◽  
Shenghua He ◽  
Walid Elfalleh ◽  
Weiyi Xu ◽  
...  

1980 ◽  
Vol 47 (2) ◽  
pp. 199-210 ◽  
Author(s):  
Donald F. Darling

SummaryThe heat stability of a standard reconstituted skim-milk preparation has been investigated as a function of pH, temperature of coagulation, and forewarming treatment. Apparent activation energies have been calculated from the temperature dependence of coagulation time, and a constant value of 144 kJ/mole has been found for milks between pH 6·6 and 6·9. The effect of forewarming resulted in a decrease in stability at the most acid pH values, a slight increase at higher pH but below the pH maximum, and a decrease in the region of the pH minimum. A working hypothesis is proposed for the mechanisms leading to the coagulation of milk at elevated temperatures, based upon Ca induced precipitation of casein, protein polymerization, β-lactoglobulin: κ-casein interaction, and precipitation of insoluble Ca phosphates.


1977 ◽  
Vol 44 (2) ◽  
pp. 249-257 ◽  
Author(s):  
D. D. Muir ◽  
A. W. M. Sweetsur

SummaryAdditions of urea progressively increased the heat stability of milk outside of its coagulation time (CT)–pH minimum. In the region of the CT–pH minimum larger amounts of urea were required before an increase in heat stability occurred. The effect of urea was observed over the temperature range 125–140 °Cfornaturalmilk, milk which had been dialysed against synthetic sera, and milk to which a sulphydrylblocking agent had been added. Urea additions did not affect the activation energy of the heat coagulation reaction or the stability of milk to rennet or ethanol.


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