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Ninhydrin reacts with ammonia, a primary amine, or a secondary amine (amino acids have a primary or alpha amino group, except for proline which has a secondary amino group). They all turn purple/blue right away upon heating with ninhydrin.

Remember that a protein has a amino terminal and a -COOH terminal. The ninhydrin will react with the amino terminal giving a very light blue or violet color (more often than not you will see no color change). Upon further heating you may notice an increase in the intensity of the blue/violet. this is due to the heat denaturing the protein, thereby exposing more -NH2 groups for the ninhydrin reagent to react with

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16y ago
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13y ago

-Absorption Spectroscopy

The Protein Peptides absorb some blue (degradation) photons and leaves a purple color.

The intensity of the resulting color, determines the amount of Protein.

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12y ago

This reagent reacts specifically to peptide bonds which are present in proteins. Amino acids are chained together by peptide bonds to make proteins.

An isolated amino acid simply will not react, as it is only a building block of a potential protein given the right circumstances (peptide bonds). ---> -C(=O)NH-

An amino acid on it's own just doesn't have the right chemical structure to react with biurets reagent.

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16y ago

i think that all proteins give a posotive biuret test because of the presence of peptide bonds

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11y ago

because it take o atom from protein 2 compose NH3

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12y ago

ninhydrine reacts with alpha amino acid which is present in both amino acid and protein

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Q: Why ninhydrin shows positive test for amino acid and protein?
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What does each word represent in terms of protein synthesis?

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