Determination of thermally-induced conformational slides in β-lactoglobulin prior to irreversible thermal denaturation

Abstract

[Excerpt] Introduction: β-lactoglobulin (β-Lg) is the major globular protein in milk and the dominant functional agent in whey and its derivatives ingredients. It is generally recognized that β-Lg undergoes conformational changes above temperatures of 60 °C and unfolds irreversibly after 70 °C. The conformational changes that happen during this process have critical implications in β-Lg functional properties, thus affecting both technological quality of milk (i.e. cheese production) and whey ingredients, which use are currently widespread in food formulations. In this study thermal effects in β-Lg have been investigated through an innovative approach, combining on-line spectroscopy techniques, aiming at achieving a more detailed characterization of these events below and above the melting temperature. [...]