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Is your Skinny ScienceB-Creamy™ Creamer clumping up
when you add it to Skinny Science's brewed Skinny Science® Coffee?

Why does the B-Creamy™ Creamer sometimes clump up when I add it to my brewed B-Skinny™ Coffee™?

It's because of mother nature!

Cow's do not give milk at the boiling point - It's only slightly warm.

At high temperatures, milk proteins, which are curled-up, begin to unfold and link together in clumps.

WHY DOES THIS HAPPEN?

If the Skinny Science® Coffee is really hot (near the boiling point) -when you add B-Creamy™ Creamer - then the natural protein molecules in B-Creamy™ can clump-up.

This can occur because when liquid dairy milk is dried into a powder, it still has all the properties of milk, so when boiling water, or water that is too hot, or hot Skinny Sciencecoffee is mixed with the B-Creamy™ Creamer, it can all clump-up.

If this clumping occurs when you make a cup of Skinny Science® Coffee, and add B-Creamy™ - there is nothing wrong with the B-Creamy™. It's just following the dictates of nature.

Skinny Sciencecould solve the problem by using artificial and unnatural chemicals to make the creamer tolerate high temperatures, but we simply won't do this.

THERE ARE 2 SIMPLE SOLUTIONS:

1) Wait until your Skinny Science® Coffee cools a bit, then add the B-Creamy™ Creamer.

2) Simply make the B-Creamy™ Creamer into a liquid by placing the desired amount of B-Creamy™ Creamer into 1 cup of warm water (not boiling hot) - stir until fully dissolved - and use as desired. This can keep in the fridge for 2 days.



FOR INQUIRING & SCIENTIFIC MINDS,
THE SCIENTIFIC EXPLANATION IS BELOW:

THE SCIENTIFIC EXPLANATION
Thermal Denaturation of Natural Milk Proteins



When proteins are exposed to increasing temperature, losses of solubility or enzymatic activity occurs over a fairly narrow range. Depending upon the protein studied and the severity of the heating, these changes may or may not be reversible.

As the temperature is increased, a number of bonds in the protein molecule are weakened. The first affected are the long range interactions that are necessary for the presence of tertiary structure. As these bonds are first weakened and are broken, the protein obtains a more flexible structure and the groups are exposed to solvent. If heating ceases at this stage the protein should be able to readily refold to the native structure.

As heating continues, some of the cooperative hydrogen bonds that stabilize helical structure will begin to break. As these bonds are broken, water can interact with and form new hydrogen bonds with the amide nitrogen and carbonyl oxygens of the peptide bonds.

The presence of water further weakens nearby hydrogen bonds by causing an increase in the effective dielectric constant near them. As the helical structure is broken, hydrophobic groups are exposed to the solvent.

The effect of exposure of new hydrogen bonding groups and of hydrophobic groups is to increase the amount of water bound by the protein molecules. The unfolding that occurs increase the hydrodynamic radius of the molecule causing the viscosity of the solution to increase. The net result will be an attempt by the protein to minimize its free energy by burying as many hydrophobic groups while exposing as many polar groups as possible to the solvent. While this is analogous to what occurred when the protein folded originally, it is happening at a much higher temperature. This greatly weakens the short range interaction that initially direct protein folding and the structures that occur will often be vastly different from the native protein.

Upon cooling, the structures obtained by the aggregated proteins may not be those of lowest possible free energy, but kinetic barriers will prevent them from returning to the native format. Any attempt to obtain the native structure would first require that the hydrophobic bonds that caused the aggregation be broken.

This would be energetically unfavorable and highly unlikely. Only when all the intermolecular hydrophobic bonds were broken, could the protein begin to refold as directed by the energy of short range interactions. The exposure of this large number of hydrophobic groups to the solvent, however, presents a large energy barrier that make such a refolding kinetically unlikely.

Exposure of most proteins to high temperatures results in irreversible denaturation. Some proteins, like caseins, however, contain little if any secondary structure and have managed to remove their hydrophobic groups from contact with the solvent without the need for extensive structure. This lack of secondary structure causes these proteins to be extremely resistant to thermal denaturation.

The increased water binding noted in the early stages of denaturation may be retained following hydrophobic aggregations. The loss of solubility that occurs will greatly reduce the viscosity to a level below that of the native proteins.







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