Thermal Denaturation of Whey Proteins Characterized by Circular Dichroism

Document Type

Student Presentation

Presentation Date



College of Arts and Sciences


Department of Chemistry & Biochemistry

Faculty Sponsor

Dr. Owen McDougal


Whey proteins are one of two categories of milk protein that are globular and therefore subject to thermal denaturation during milk processing (pasteurization, spray drying, etc.). Dairy product manufacturers have an interest in the development of rapid, economical, and accurate methods for monitoring the degree of whey protein denaturation. The question addressed by this research is: “Can circular dichroism (CD) spectroscopy be used to accurately characterize secondary structural changes associated with protein denaturation in whey proteins over a range of temperatures?” Using CD spectroscopy and the associated online database, four primary whey proteins: β-lactoglobulin, α-lactalbumin, bovine serum albumin, and immunoglobulin G, were analyzed from 20-90 °C, and percentages of various secondary structural elements, including alpha helix, beta strand, beta turn, and unordered components were determined. From the data we can demonstrate the temperature at which each protein component of whey dramatically changes, indicating the point at which denaturation occurs. We will use CD analysis to develop a robust method to rapidly monitor whey protein denaturation. The CD method will be complemented by protein separation using high performance liquid chromatography and optical spectroscopy techniques (IR and UV-Vis) to validate results.

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