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Updated: May 27, 2026
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Scanning calorimetric studies on offal protein isolates
1Department of Applied Biochemistry and Food Science, School of Agriculture, University of Nottingham, Sutton Bonington, Loughborough, Leicestershire, LE 12 5RD, Great Britain.
Abstract:
Differential scanning calorimetry was performed on protein isolated from bovine lung and rumen. Isolates defatted with solvents of increasing polarities (petroleum ether, carbontetrachloride, chloroform, dichloromethane, isopropanol, ethanol and methanol) presented very similar phase transitions. The thermograms of the original, non-defatted rumen isolates exhibited phase transitions which recovered completely after incubation at 303-313 K. This reversible effect was not noticed after petroleum ether extraction. Mixture and incubation at 313 K of the defatted proteins and the extracted fat fraction failed in reproducing the reversibility observed.
