Related Experiment Video
Updated: Feb 22, 2026

Comparison of Tobacco Host Cell Protein Removal Methods by Blanching Intact Plants or by Heat Treatment of Extracts
Published on: August 8, 2016
Tracking hydrophobicity state, aggregation behaviour and structural modifications of pork proteins under the
Bhaskar Mitra1, Åsmund Rinnan1, Jorge Ruiz-Carrascal1
1Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
Abstract:
Structural modifications of pork proteins under an assortment of industrial heat treatments were studied. With raw as control, assorted heat treatments involved were 58, 80, 98 and 160°C for 72min, 118°C for 8min and 58°C for 17h, resembling most common processing procedures. Protein denaturation, surface protein hydrophobicity state and protein aggregation behaviour were investigated. Modifications and molecular chemistry in protein structures were tracked by Fourier Transform Infrared Spectroscopy in order to extract relative proportions of β-sheet, α-helix and residual conformations. In comparison to uncooked samples, cooked ones showed more than two-fold increase in hydrophobicity and larger particles. Thermograms from differential scanning calorimetry showed endothermic transitions (positive enthalpy) indicating a different pattern of protein denaturation as a result of varied cooking temperatures and cooking times. Deconvolution and curve fitting procedures (R2=0.99) provided information on rise of the β-sheet to α-helix ratio that further confirmed aggregation with thermal rise and longer cooking time.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Protein Denaturation
Bacterial Protein Maturation
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...

