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Food Chem. 2013 Aug 15;139(1-4):611-6. doi: 10.1016/j.foodchem.2013.01.073. Epub 2013 Feb 9.

Probing the binding between norbixin and dairy proteins by spectroscopy methods.

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1
Department of Food Science and Technology, University of Tennessee, Knoxville, United States.

Abstract

Annatto (norbixin) has been used to color cheeses for centuries, but there is very little knowledge about interactions between the pigment and dairy proteins. In this study, binding of norbixin with whey protein isolate (WPI), sodium caseinate (NaCN), and 6 individual dairy proteins was investigated by using fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) and differential scanning calorimetry (DSC). Norbixin was observed to effectively quench the fluorescence of WPI and NaCN by forming complexes. The binding affinity between NaCN and norbixin was higher than that of WPI-norbixin. For individual proteins, bovine serum albumin had higher binding affinity with norbixin than β-lactoglobulin and α-lactalbumin, while κ-casein bound with norbixin better than α- and β-caseins. Binding changed the conformation of WPI and NaCN, but the extent and trend varied for individual proteins.

PMID:
23561152
DOI:
10.1016/j.foodchem.2013.01.073
[Indexed for MEDLINE]
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