Abstract
We present a preliminary report on the use of plant dyes in the quantitation of proteins in solution. We have used ethanol, acid, alkali and water to extract dyes from some plant materials, including flowers of Jungle flame (Izora coccinea), China rose (Hibiscus rosa-sinensis) and leaves of West African Indigo (Lonchocarpus cyanescens), Mimosa (Mimosa pudica), Roselle (Hibiscus sabdarifa), Jatropha (Jatropha curcas) and Henna (Lawsonia inermis). The dyes obtained were used in the protein-dye binding studies. The colour of the protein-dye complex of the ethanolic extracts was stable and increased linearly with increase in protein concentration. The extracts achieved linearity up to the following amount of proteins in the test samples: Hibiscus rosa-sinensis (60 mg), Ixora coccinea (120 mg), Hibiscus sabdarifa (80 - 100 mg), Jatropha curcas (80 mg), and Lawsonia inermis (100 mg). The sensitivity of the dyes especially at low protein concentrations indicate that they can provide suitable alternatives to other well known standard methods of protein determination.
Highlights
There are currently many methods to quantify proteins in solution
We present a preliminary report on the use of plant dyes in the quantitation of proteins in solution
Apart from the insensitivity, other main disadvantages of this method in protein measurements are that the presence of salts e.g. (NH4)2SO4 carry over, or other substances which might be present in protein solution affect colour development and the overall result of protein concentration obtained
Summary
There are currently many methods to quantify proteins in solution. Some are quite insensitive and can detect proteins only in the milligram range, whereas others are very sensitive and can be used to measure proteins as low as 5 - 10 g in solution. Apart from the insensitivity, other main disadvantages of this method in protein measurements are that the presence of salts e.g. Protein quantitation using Folin-phenol reagent [2], can detect protein in solution at concentrations as low as 5 - 10 g. The reaction is pH dependent and as such protein solution that contains some of the materials mentioned, cannot be correctly measured. Protein solutions with fewer aromatic amino acids would have a lowered absorbance and the method appears relatively cumbersome
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