A Simple Fluorometric Method for Fat‐Binding Capacity as an Index of Hydrophobicity of Proteins
- 1 September 1986
- journal article
- research article
- Published by Wiley in Journal of Food Science
- Vol. 51 (5) , 1268-1272
- https://doi.org/10.1111/j.1365-2621.1986.tb13102.x
Abstract
A new procedure was established for determining fat‐binding capacity of proteins, using a nonpolar fluorescent probe diphenylhexatiene dissolved in corn oil. The amount of bound oil was measured from the fluorescence intensity (FI) of the bottom layer after centrifuging the blended protein‐oil‐probe mixture. This method classified proteins into two groups, i.e., group 1 which had FI increasing linearly with protein concentration and group 2 which had FI increasing then decreasing. The linearly fitted slope of the FI‐protein plot revealed better correlation with anilinonaphthalenesulfonate hydrophobicity than with cis‐parinarate hydrophobicity. It also showed a significant correlation with emulsifying activity index.This publication has 3 references indexed in Scilit:
- Relationships of Hydrophobicity and Net Charge to the Solubility of Milk and Soy ProteinsJournal of Food Science, 1985
- The relationship between hydrophobicity and interfacial tension of proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic seriesArchives of Biochemistry and Biophysics, 1977