Abstract
Structural Properties of Casein Micelles in Milk, the effect of salt, temperature, and pH
Highlights
Milk is as ancient as human beings themselves
Milk is a complex liquid, which contains many different species, for example proteins, fat, minerals etc. It is the primary source of nutrition for young mammals before they are able to digest other types of food
There might be an influence of the electric permittivity since it was kept constant during the simulations, When the salt concentration was increased to 80 mM, which corresponds to the ionic strength in milk, the structure of the β -casein micelles resembles the structure of an ideal gas i.e. the electrostatic repulsive interactions are screened
Summary
Milk is as ancient as human beings themselves. Historians believe that humans started to drink milk over 10,000 years ago, along with the start of the domestication of animals. 2)UHT: ultra high temperature pasteurization, which requires heating the liquid to 1380 C for 2 seconds, and can extend the shelf life for weeks It causes some changes of the structure of the milk protein.[2]. There are 20 amino acids, which form the different protein types where 9 of them are essential for diet and all of which are present in milk. Both alpha and beta casein are attached to the cluster. < z > is the net average charge of the protein
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