Interactions between puerarin/daidzein and micellar casein

Author(s):  
Yucheng Wang ◽  
Min Yang ◽  
Juanjuan Qin ◽  
Wenqiang Wa
Keyword(s):  
1979 ◽  
Vol 46 (2) ◽  
pp. 291-306 ◽  
Author(s):  
Theodoor A. J Payens

SUMMARYThe colloidal properties of micellar casein are reviewed. It is shown that the behaviour of intact micelles is much at variance with the predictions from the Schulze–Hardy rule, and that therefore their stability cannot be explained by the principles of the DLVO theory. Towards electrolyte, micelles behave as a protein rather than a lyophobic colloid.Casein is a strong protective colloid. In the micelle, however, it does not completely cover the inorganic constituent which remains sensitive to changes in the ionic environment.The rate theory of the enzyme-induced clotting of casein micelles is summarized. It is shown that the lag phase in the clotting is due to the second order of the coagulation reaction. Flocculation rate constants of micelles have been deduced from clotting times. Their relatively low values can be attributed to an orientational constraint. Practical consequences of the theory with respect to clot structure, gelation of sterilized products and cheese manufacture are discussed.


LWT ◽  
2021 ◽  
pp. 111935
Author(s):  
Xinqi Zhao ◽  
Cunfang Wang ◽  
Ming Cheng ◽  
Xiaoning Zhang ◽  
Hua Jiang
Keyword(s):  

2012 ◽  
Vol 26 (2) ◽  
pp. 112-119 ◽  
Author(s):  
Esther de Kort ◽  
Marcel Minor ◽  
Thom Snoeren ◽  
Toon van Hooijdonk ◽  
Erik van der Linden

2016 ◽  
Vol 27 (10) ◽  
pp. 3103-3112 ◽  
Author(s):  
A. Boulier ◽  
J. Schwarz ◽  
E. Lespesailles ◽  
A. Baniel ◽  
D. Tomé ◽  
...  

Author(s):  
Xiaofeng Xia ◽  
John T Tobin ◽  
Mark A Fenelon ◽  
Paul L H Mcsweeney ◽  
Jeremiah J Sheehan

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.


2020 ◽  
Vol 107 ◽  
pp. 104711
Author(s):  
Bozhao Li ◽  
David S. Waldron ◽  
John T. Tobin ◽  
Surabhi Subhir ◽  
Alan L. Kelly ◽  
...  

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