Intrinsic Fluorescence as a Spectral Probe for Protein Denaturation Studies in the Presence of Honey
Honey was found to quench the intrinsic fluorescence of bovine serum albumin (BSA) in a concentration dependent manner, showing complete quenching in the presence of 5% (w/v) honey. Increasing the protein concentration up to 5.0 μM did not lead to the recovery of the protein fluorescence. Urea denat...
Main Authors: | Wong, Y.H., Kadir, H.A., Tayyab, S. |
---|---|
Format: | Article |
Published: |
Kluwer (now part of Springer)
2015
|
Subjects: |
Similar Items
-
Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence
by: Wong, Y.H., et al.
Published: (2013) -
Targeting chemical and thermal stability of ovalbumin by simulated honey sugar cocktail
by: Wong, Y.H., et al.
Published: (2015) -
Alcohol-induced structural transitions in the acid-denatured Bacillus licheniformis α-amylase
by: Halim, A.A.A., et al.
Published: (2017) -
Effect of Various Polyols on the Acid-Denatured States of Champedak Galactose-Binding Lectin
by: Kameel, Nurul Iman Ahamed, et al.
Published: (2018) -
Probing the hydrophobic sites on the surface of serum albumins using bromophenol blue-induced fluorescence quenching: A comparative study
by: Boh, B.K., et al.
Published: (2007)