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Updated: Jun 28, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Conformational changes in bovine lactoferrin induced by slow or fast temperature increases
Waleska D Schwarcz1, Lorena Carnelocce, Jerson L Silva
1Mestrado em Ciência e Tecnologia do Leite, Universidade Norte do Paraná, 86041-100 Londrina, PR, Brazil.
Heat affects bovine lactoferrin (LF) structure, altering its tertiary but not secondary structure during pasteurization. This suggests LF may form a partially folded state, impacting its use in food products.
Area of Science:
- Biochemistry
- Food Science
- Protein Chemistry
Background:
- Lactoferrin (LF) is an iron-binding protein with antimicrobial and physiological functions, found in milk.
- Protein stability and functionality can be compromised by high temperatures, affecting its applications.
Purpose of the Study:
- To investigate the impact of heat on the structure and stability of bovine lactoferrin (LF).
- To understand how pasteurization temperatures affect LF's protein functionality.
Main Methods:
- Spectroscopic techniques, including circular dichroism (CD) and fluorescence spectroscopy, were used to monitor conformational changes.
- Simulated pasteurization processes were employed to assess LF stability under relevant conditions.
Main Results:
- Elevated temperatures (e.g., 70°C and 25°C–105°C) drastically and irreversibly altered LF's secondary structure, as shown by CD and fluorescence spectroscopy.
- During simulated pasteurization, LF maintained structural integrity, indicating heat stability that was not time-dependent.
- While secondary structure was preserved, tertiary structure changes suggested LF might transition to a partially folded intermediate state.
Conclusions:
- Pasteurization may induce a partially folded state in bovine lactoferrin, altering its tertiary structure.
- Understanding the heat stability of LF is crucial for its effective utilization as a bioactive component in food products.
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