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I did a Biochemistry lab on absorbance using ninhydrin with Tyrosine and Glycine. Their absorbance was then measured at 570nm. The absorbance values obtained for tyrosine and glycine were 0.280 and 1.247 respectively.

What could have accounted for the significant difference in absorbance values if the same volume of amino acid solution and ninhydrin were used?

Respuesta :

The solutions of amino acids have different concentrations.

Explanation:

To determine the concentrations of molecules by measuring their absorbance dissolved solution you use the Lambert-Beer law which states that:

A = ε × l × c

where:

A = absorbance

ε = absorptivity

c = concentration

l = optical path length

The difference in the absorbance values is given by the different concentrations of the amino acids solutions. The reactions of ninhydrin with the amino acids yields the same molecule (ε will not change) so the  that gives the color so the absorbance peak is not shifted when you detect different aminoacid molecules. Of course I assume that the byproducts in the chemical reaction will not have a absorption band in the UV-Vis spectra at 570 nm.

Lean more:

about Lambert-Beer law

brainly.com/question/3912394

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