Abstract
Ponceaue 4R interaction with protein, Nisin and BSA was concentration dependent and may be used for protein assay. As the dye binds with almost all the proteins and current methodology may be used for the estimation of proteins in various food systems. During the course of present work staining with ponceau 4R of resolved proteins on PAGE (poly acryl amide gel electrophorosis) was comparable with Coommassie Brilliant Blue R250. The Ponceaue 4R was highly sensitive, rapid and produced sharp red bands on the gel on 0.2% concentration. The effects of pH, concentration of proteins and dye were also investigated in various conditions which would help food processors to use a calculated amount of dye. The impact of tryptic digestibility on Ponceaue 4R -Protein Complexes (PPC) has illustrated that dye may safely be used without any adverse effect on the digestion of PPC.
Highlights
It is an age old practice to enhance food quality and its aesthetical appeal by incorporation of edible colors in a variety of food systems like candy, marshmallow, soft drink, vermicelli etc
The present study is illustrating through PAGE shows the strong binding potential with various food proteins
The protein bands in case of Ponceau 4R are lighter but they appear to be very sharp at 0.2% concentration than Coomassie brilliant blue R-250
Summary
It is an age old practice to enhance food quality and its aesthetical appeal by incorporation of edible colors in a variety of food systems like candy, marshmallow, soft drink, vermicelli etc. Synthetic colorants with wide chemical diversity represent a well recognized group of food additives, performing the prime function not just to compensate the loss of natural colors during processing and improving the appearance of the products. Many of these dyes lead to health hazards (Downham & Collins, 2000) as indicated by the World Health Organization (WHO) and Food and Agriculture Organization (FAO). Inclusion complexes of some azo dyes with β-cyclodextrins are reported to be formed as illustrated by X-ray diffraction and UV spectrophotometery (Pardo et al, 2009). Natural flavonoids and carotenoids are reported to bind with proteins both in vivo and in vitro (Wade, Tollenaere, Hall, & Degnan, 2009)
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