Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence

Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe. BSA was labelled with FITC using chemical coupling, and urea and thermal denaturation studies were performed on FITC-labe...

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Main Authors: Wong, Y.H., Abdul Kadir, H., Tayyab, S.
Format: Article
Language:English
Published: Hindawi Publishing Corporation 2013
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Online Access:http://eprints.um.edu.my/8581/1/3.pdf
http://eprints.um.edu.my/8581/
http://www.ncbi.nlm.nih.gov/pubmed/24222758
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spelling my.um.eprints.85812017-07-06T00:56:18Z http://eprints.um.edu.my/8581/ Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence Wong, Y.H. Abdul Kadir, H. Tayyab, S. R Medicine Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe. BSA was labelled with FITC using chemical coupling, and urea and thermal denaturation studies were performed on FITC-labelled BSA (FITC-BSA) both in the absence and presence of 10% and 20% (w/v) honey using FITC fluorescence at 522 nm upon excitation at 495 nm. There was an increase in the FITC fluorescence intensity upon increasing urea concentration or temperature, suggesting protein denaturation. The results from urea and thermal denaturation studies showed increased stability of protein in the presence of honey as reflected from the shift in the transition curve along with the start point and the midpoint of the transition towards higher urea concentration/temperature. Furthermore, the increase in ΔG D (H2O) and ΔG D (25°C) in presence of honey also suggested protein stabilization. Hindawi Publishing Corporation 2013 Article PeerReviewed application/pdf en http://eprints.um.edu.my/8581/1/3.pdf Wong, Y.H. and Abdul Kadir, H. and Tayyab, S. (2013) Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence. Scientific World Journal. ISSN Hindawi Publishing Corporation http://www.ncbi.nlm.nih.gov/pubmed/24222758
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
language English
topic R Medicine
spellingShingle R Medicine
Wong, Y.H.
Abdul Kadir, H.
Tayyab, S.
Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
description Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe. BSA was labelled with FITC using chemical coupling, and urea and thermal denaturation studies were performed on FITC-labelled BSA (FITC-BSA) both in the absence and presence of 10% and 20% (w/v) honey using FITC fluorescence at 522 nm upon excitation at 495 nm. There was an increase in the FITC fluorescence intensity upon increasing urea concentration or temperature, suggesting protein denaturation. The results from urea and thermal denaturation studies showed increased stability of protein in the presence of honey as reflected from the shift in the transition curve along with the start point and the midpoint of the transition towards higher urea concentration/temperature. Furthermore, the increase in ΔG D (H2O) and ΔG D (25°C) in presence of honey also suggested protein stabilization.
format Article
author Wong, Y.H.
Abdul Kadir, H.
Tayyab, S.
author_facet Wong, Y.H.
Abdul Kadir, H.
Tayyab, S.
author_sort Wong, Y.H.
title Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
title_short Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
title_full Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
title_fullStr Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
title_full_unstemmed Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
title_sort honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
publisher Hindawi Publishing Corporation
publishDate 2013
url http://eprints.um.edu.my/8581/1/3.pdf
http://eprints.um.edu.my/8581/
http://www.ncbi.nlm.nih.gov/pubmed/24222758
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