Boiling A2 milk does not destroy nutrients (or useful enzymes) provided you do it in low flame for extended time.

Basically, you are giving an opportunity to enzymes to adapt to new state.

Curd is more nutritious than milk.

Once you churn curd manually by adding water twice or thrice volume of curd, we get buttermilk and butter which are independently more nutritious than curd.

Again under low flame, butter is converted to ghee whose nutrition cannot be matched with any other food

empoweredsustenance.com/raw-milk-is-special

Hi, A1, A2  usually they are proteins in nature ,therefore boiling (100 C) denaturation   them  and destroy and the solvent by Pasturization

 i think that Heating results in a slight decrease in several vitamins, but this loss is not significant from a health perspective

Dear Shridhar

Please, see the following link, I hope will be useful for you.

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1975518/pdf/archdisch01478-0039.pdf

Good Luck

J. Agric. Food Chem. 1981, 29, 11-15 11

Effects of Ultra-High-Temperature Pasteurization on Milk Proteins

Frederic W. Douglas, Jr.,* Rae Greenberg, Harold M. Farrell, Jr., and Locke F. Edmondson'

Ultra-high-temperature (UHT) pasteurization of skim milk (148 "C for 3 s) has been found to inactivate

effectively foot and mouth disease virus. For determination of the effect of UHT pasteurization on milk

proteins, the composition and properties of proteins from milk after this treatment were compared with

those from conventional high-temperature-short-time pasteurized (HTST = 71.7 "C for 15 s) and raw

skim milks. Vacuum-dried-acid-precipitated caseins and freeze-dried-dialyzed whey proteins were

prepared from each product. Functional properties of casein such as solubility, viscosity, emulsifying

capacity, and electrophoretic mobility were compared. For both casein and whey proteins, compositional

comparisons were made among molar ratios of amino acids, total protein, and chemically available lysine.

The solubility of milk caseins was reduced by UHT pasteurization. Whey protein nitrogen analyses

show significant protein denaturation. No significant losses in nutritive value are indicated, and differences

in viscosity and emulsification capacity are small.

Earlier studies (Burrows and Dawson, 1968; Hedger and

Dawson, 1970; Sellers, 1969; Terbriiggen, 1932) indicated

that the virus from foot and mouth disease (FMD) infeded

cows can survive in milk and derived milk products such

as cheese (Blackwell, 1975) and casein (Cunliffe and

Blackwell, 1977). FMD virus in whole milk, skim milk, and

cream from experimentally infected dairy cows (Blackwell

and Hyde, 1976) can survive conventional high-temperature-

short-time (HTST = 71.7 "C for 15 s) pasteurization.

Cunliffe et al. (1978, 1979) showed the persistence of infectious

FMD virus up to 42 days in heat-dried caseins

produced by acid precipitation of HTST-pasteurized skim

milk from infected cows. Milk-borne FMD virus may pose

a serious threat to FMD-free countries, and reliable procedures

are needed to inactivate FMD virus in milk. Heat

treatments considerably above pasteurization have been

referred to as ultra-high-temperature (UHT) processes.

According to the International Dairy Federation (1972),

UHT processes refer to pasteurization techniques with

temperatures of at least 130 "C in a continuous flow and

holding times of -1 s or more. Cunliffe et al. (1979)

reported that UHT pasteurization effectively inactivates

FMD virus in milk when carried out at 148 "C for 3 s or

longer. It was of interest to determine the effect of this

regimen on the properties of caseins and whey proteins

prepared from UHT-pasteurized skim milk and to compare

them with those prepared from HTST-pasteurized and raw

skim milk. The results indicated that UHT pasteurization

Eastern Regional Research Center, Agricultural Research,

Science and Education Administration, US. Department

of Agriculture, Philadelphia, Pennsylvania

19118.

'

Hi Shridhar,

Beta casein is a major milk protein (concentration is approx. 9g/litre of milk) with 206 amino acids. In A1 milk, beta-casein protein has histidine in 67th position while A2 has proline in that position. When we drink milk, upon proteolytic degradation, A1 beta casein releases Beta casomorphine-7 (BCM-7) while A2 does not. It is the BCM-7 that causes public health concern as it is proposed to predispose various health issues (yes, that is the science behind A1 and A2 issue!)

Coming to the question, heat treatment generally does not break the primary amino acid structure of proteins. Let us see what happens when you heat milk. Milk proteins when heated, undergo denaturation. Denaturation takes place in two steps. The first step is unfolding of native structure. Here, hydrophobic residues and disulphide bonds are exposed. But, remember, the unfolded proteins can refold into native structure, if heating is minimal. At very high temperatures, the unfolded proteins will refold by forming new hydrophobic bonds and disulphide bridges. This refolding is not into its native conformation but to a random structure. The second step of denaturation at very high temperature is the formation of aggregates with other molecules by forming disulphide and covalent bonds.

With regard to A1 and A2, caseins are very heat resistant due to their loose structure. Their primary chain is hard to break. They can tolerate very high temperature. But of course, secondary and tertiary structures are heat labile. So, heat treatment may not destroy A1 or A2.

Hence, heat treatment may not destroy A1 or A2 in milk.

No.

The breed of cow your milk comes from may make a major difference in whether or not it's healthy. ... which entails heating the milk to a temperature of 145 degrees to ..... Telling people to use jersey milk will not in the least guarantee A2 milk. .... Hence a truly healthy person can probably tolerate A1 milk.

Hi

The breed of the animal can tell us about A1 and A2. Bos indicus breeds are generally A2 genotype.Among taurine breeds, Jersey animals are mostly A2. A2 is the wild type. The A2 to A1 mutation happened some 10,000 years back.

A1 animals produce more milk compared to A2 animals ( see my article: https://www.researchgate.net/publication/311651744_BETA_CASEIN_A1A2_POLYMORPHISM_AND_MILK_YIELD_IN_VECHUR_KASARGODE_DWARF_AND_CROSSBRED_CATTLE_1_2). So intensive selection for milk production in high yielding animals would have increased A1 proportion in them. 

As to consumption of A1 milk, healthy adult people can, of course, tolerate BCM-7 that is released by A1 milk digestion. But, for infants, it is better to avoid, because, in infants, smaller peptides are directly absorbed from GI tract. That is the case with calves too. Vets recommend not to overfeed milk to the calves.

Article BETA CASEIN A1A2 POLYMORPHISM AND MILK YIELD IN VECHUR, KASA...

Thanks to all for answering