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Fluorescence spectroscopy as a tool for monitoring solubility and aggregation behavior of β‐lactoglobulin after heat treatment
Author(s) -
Elshereef Rand,
Budman Hector,
Moresoli Christine,
Legge Raymond L.
Publication year - 2006
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.21039
Subject(s) - solubility , chemistry , fluorescence spectroscopy , whey protein , protein aggregation , fluorescence , denaturation (fissile materials) , chromatography , ingredient , fluorescence anisotropy , active ingredient , analytical chemistry (journal) , biological system , organic chemistry , food science , biochemistry , physics , quantum mechanics , membrane , nuclear chemistry , bioinformatics , biology
Denaturation and aggregation of whey proteins are of interest to the food and pharmaceutical industry due to the importance of final structure in functionality, impact on food texture, and the chemical stability of the final product. In this study, we demonstrate the potential of fluorescence spectrometry combined with multivariate chemometric methods for quantifying solubility and aggregation behavior of β‐lactoglobulin (β‐LG); a major whey protein and a frequent food ingredient. Heat‐induced aggregation of β‐LG was studied under different conditions including pH, temperature and heating durations. Results showed very good agreement between the fluorescence‐based predictions and measurements obtained by HPLC and gravimetric analysis regardless of the conditions. Standard normal variate (SNV), a signal preprocessing and filtering tool, was found to enhance the predictive accuracy and robustness of the fluorescence‐based model. © 2006 Wiley Periodicals, Inc.