pH and heat-induced structural changes of bovine apo-α-lactalbumin |
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Authors: | Nicoleta St?nciucGabriela Râpeanu Gabriela BahrimIuliana Aprodu |
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Affiliation: | University “Dun?rea de Jos” of Galati, Faculty of Food Science and Engineering, 111 Domneasca Street, 800201 Galati, Romania |
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Abstract: | The effects of pH and thermal treatments on conformation and association state of Ca2+-depleted bovine α-lactalbumin (apo-α-LA) have been studied by fluorescence spectroscopy, and molecular modelling. The experimental results demonstrate a third-state model for heat-induced unfolding of apo-α-LA, at pH 2.0, and an all-or-none transition of apo-α-LA, at pH 4.5 and 7.0, respectively. The heat-induced changes in the secondary and tertiary structure of α-LA were outlined after running molecular dynamics simulations at 25 °C and 80 °C, at neutral pH, therefore supporting the experimental observations. Our data provides insight into the mechanism of pH- and heat-dependent structural changes and oligomerization of α-LA, and will be helpful in understanding the ability of this protein to interact with certain compounds of biological interest. |
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Keywords: | apo-α-LA apo-α-lactalbumin ANS 8-anilino-1 naphthalenesulfonic acid MG molten globule KSV Stern-Volmer quenching constants |
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