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  2. Casein - Wikipedia

    en.wikipedia.org/wiki/Casein

    Sheep and cow milk have a higher casein content than other types of milk with human milk having a particularly low casein content. [2] Casein is the primary emulsifier in milk, that is, it helps in mixing oils, fats, and water in milk. [3] Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. [4]

  3. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  4. Maillard reaction - Wikipedia

    en.wikipedia.org/wiki/Maillard_reaction

    They are both promoted by heating, but the Maillard reaction involves amino acids, whereas caramelization is the pyrolysis of certain sugars. [ 14 ] In making silage , excess heat causes the Maillard reaction to occur, which reduces the amount of energy and protein available to the animals that feed on it.

  5. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. [3] [4] It is called tyrosyl when referred to as a functional group or side chain.

  6. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids have zero mobility in electrophoresis at their isoelectric point, although this behaviour is more usually exploited for peptides and proteins than single amino acids. Zwitterions have minimum solubility at their isoelectric point, and some amino acids (in particular, with nonpolar side chains) can be isolated by precipitation from ...

  7. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and chemical reactivity. [32] The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl

  8. Whey - Wikipedia

    en.wikipedia.org/wiki/Whey

    Whey protein has a high level of leucine, [21] one of the three branched-chain amino acids, making it ideal for muscle growth and repair. [citation needed] [22] Whey is pasteurized to assure that no harmful bacteria are breeding in the liquid. It is heated to 70–80 °C (158–176 °F) and is then cooled back down to 4 °C (39 °F).

  9. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structures range in size from tens to several thousand amino acids. [2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.