Fluorescence spectroscopy and molecular modeling investigations on the thermally induced structural changes of bovine β-lactoglobulin
作者： Nicoleta Stănciuc , Iuliana Aprodu , Gabriela Râpeanu , Gabriela Bahrim
DOI: 10.1016/J.IFSET.2012.03.001
关键词: Analytical chemistry 、 Molecular model 、 Quenching (fluorescence) 、 Molecular dynamics 、 Fluorescence spectroscopy 、 Whey protein 、 Tryptophan 、 Protein tertiary structure 、 Fluorescence 、 Chemistry 、 Biophysics
摘要: Abstract The heat-induced conformational and structural changes in β-lactoglobulin were analyzed using the fluorescence techniques molecular modeling approach. experimental results confirm a two-state model for of at pH 6.5. heat treatment temperatures higher than 70 °C caused an increase both intrinsic ANS intensity. addition quenching agents was employed to discriminate contributions two tryptophan residues (Trp 19 Trp 61 ). acrylamide KI causes constants associated with . This effect is observed all studied, but stronger 70 °C. secondary tertiary structure outlined after running dynamics simulations different neutral pH, therefore supporting observations. Industrial relevance In food industry, one major concerns whey processors produce protein products (such as concentrates or isolates well fractions enriched α-lactalbumin) specific functionalities. this sense, potential use supplement special has encouraged study its physico-chemical biological properties.
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