Understanding Casein's Reaction in Water: pH 4.6 Residue Formation

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SUMMARY

Casein produces a residue in water at pH 4.6 due to its isoelectric point (pI) being reached, where the concentrations of positively and negatively charged amino acid forms are equal. At this pH, the absence of repulsive forces allows the R-groups of amino acids in Casein to attract each other through van der Waals bonds, facilitating aggregation. This phenomenon is critical for understanding protein behavior in various pH environments, particularly in food science and biochemistry.

PREREQUISITES
  • Understanding of protein structure and amino acid composition
  • Knowledge of pH and isoelectric point (pI) concepts
  • Familiarity with van der Waals forces and protein interactions
  • Basic chemistry of protein solubility in aqueous solutions
NEXT STEPS
  • Research the role of isoelectric points in protein solubility and precipitation
  • Study the effects of pH on protein structure and function
  • Explore van der Waals forces in molecular interactions
  • Investigate the applications of Casein in food science and dairy products
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Students in biochemistry, food scientists, and anyone interested in protein chemistry and its applications in various industries.

vilhelm
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What happens when you put protein in water?

I know that an amino acid in water vill dissolve into:
^{+}H_3 N-CHR-COO^{-}
As protein is built up by over 50 amino acids, will the very same thing (as the formula above) happen to it?

(My homework is to explain why Casein produces a residue when put into a water solution with pH≈4,6)
 
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Protein is in a way similar to a single amino acid. You should be able to see it if you draw a simple protein, say GlyGlyGly.
 
I think this is the answer to the question why Casein produces a residue when put into a water solution with pH≈4,6 (but I'm very uncertain)

At that pH, this is what happens:

H_2N-CHR-COOH \rightarrow ^{+}H_3N-CHR-COO^{-} (Amino acid put into water solution)

pH ≈ pI \Rightarrow [^{+}H_3N-CHR-COOH] = [H_2N-CHR-COO^{-}]

This leads us to the fact that there are no repulsive forces between the amino acids, thus the R-group of the amino acids of Casein are able to attract each other via van der Waals-bonds.
When pH≠pI the protein can not come together, because of the repulsive forces.

Correct, or incorrect?
 

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