Pressure denaturation of β-lactoglobulin: Volume changes for genetic A and B variants

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Using densitometry of the partial molar volume in dilute aqueous solution at 25 °C, the genetic variant A of bovine β-lactoglobulin was found to be larger than the genetic variant B by 101.0 mL mol−1. Moderate high hydrostratic pressure increased the partial molar volume of the A-variant and B-variant up to 1.5% and 2.0%, respectively, with 30 min holding time. The observed changes in volume were not related to thiol/disulphide exchange and polymerisation reactions, but were a consequence of an increasing water binding at the protein surface in balance with an increasing water binding of the exposed protein interior. The effect was larger for the A-variant in agreement with its lower denaturation temperature and less robustness against enzymatic hydrolysis. Pressure denaturation of the β-lactoglobulin variants occurs, despite pressure-induced protein volume increase, resulting from an increase in water binding with an overall decrease in reaction volume for the denaturation process.
Original languageEnglish
Article number105416
JournalInternational Dairy Journal
Number of pages6
Publication statusPublished - 2022

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