IDEAS home Printed from https://ideas.repec.org/a/caa/jnlcjf/v28y2010i6id112-2009-cjfs.html
   My bibliography  Save this article

Food protein: Food colour interactions and its application in rapid protein assay

Author

Listed:
  • S. M. Ghufran Saeed

    (Department of Food Science & Technology)

  • S. Umer Abdullah

    (Division of Food Research, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi, Pakistan)

  • S. Asad Sayeed

    (Department of Food Science & Technology)

  • Rashida Ali

    (Division of Food Research, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi, Pakistan)

Abstract

The uniform distribution of colours as additives in a majority of the food systems is a reliable indication that one or more components of foods are able to bind with colour molecules and act as their carriers. However, the food components acting as the colour carriers have not been identified. The present paper describes the binding capacity of Carmoisine with a variety of food proteins, our results have shown that the intensity, staining, and sharpness of the stained protein bands were excellent as compared to Coomassie Brilliant Blue-R-250, which is an established staining agent for visualising electrophoretically resolved proteins. The data illustrates that Carmoisine is a fast reacting dye forming colour-complexes with all types of food proteins including curry leaves proteins. The protein bands are visualised within an hour which is useful for the initial immediate protein identifications. The experiments related to the staining of the resolved proteins with Carmoisine have shown that the dye is highly sensitive, rapid, and lasting. The food-dye can provide a quick protein assay as often desired in research works, the results may be later confirmed by using Coomassie if so required. In view of its strong binding with almost all proteins, it was thought that human proteases present in the digestive tract may not hydrolyse the bound proteins completely and may restrict the proteolytic digestion. However, the experiments based on the tryptic digestibility in vitro revealed that colour binding has no adverse effect on hydrolysis of peptide bonds by the intestinal proteases.

Suggested Citation

  • S. M. Ghufran Saeed & S. Umer Abdullah & S. Asad Sayeed & Rashida Ali, 2010. "Food protein: Food colour interactions and its application in rapid protein assay," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 28(6), pages 506-513.
  • Handle: RePEc:caa:jnlcjf:v:28:y:2010:i:6:id:112-2009-cjfs
    DOI: 10.17221/112/2009-CJFS
    as

    Download full text from publisher

    File URL: http://cjfs.agriculturejournals.cz/doi/10.17221/112/2009-CJFS.html
    Download Restriction: free of charge

    File URL: http://cjfs.agriculturejournals.cz/doi/10.17221/112/2009-CJFS.pdf
    Download Restriction: free of charge

    File URL: https://libkey.io/10.17221/112/2009-CJFS?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Jiahui JIN & Xiaodan WANG & Yunxiu HAN & Yaoxuan CAI & Yingming CAI & Hongmei WANG & Lingtao ZHU & Liping XU & Lei ZHAO & Zhiyuan LI, 2016. "Combined beef thawing using response surface methodology," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 34(6), pages 547-553.

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:caa:jnlcjf:v:28:y:2010:i:6:id:112-2009-cjfs. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Ivo Andrle (email available below). General contact details of provider: https://www.cazv.cz/en/home/ .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.