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Protein Engineering for Construction Material Performance: Effect of Protein Denaturation on Air-Entraining Function
Mohammad Sadegh Tale Masoule1, Joshua Prabahar1, Christopher Elliott Gottleib1
1Department of Civil and Architectural Engineering, University of Miami, Coral Gables, Florida 33146, United States.
Denaturing agents like sodium dodecyl sulfate (SDS) and lignin can modify protein structure, significantly enhancing air-entraining performance and freeze-thaw resistance in cement paste. Controlled protein unfolding is key to improving cement durability.
Area of Science:
- Materials Science
- Protein Chemistry
- Civil Engineering
Background:
- Proteins are used as air-entraining agents in cement paste.
- Denaturing agents can alter protein structure and properties.
- Understanding these interactions is crucial for optimizing cement performance.
Purpose of the Study:
- To investigate how denaturing agents (sodium dodecyl sulfate, urea, lignin) affect protein structure.
- To evaluate the impact of protein denaturation on air-entraining properties in cement paste.
- To assess the influence on cement paste microstructure and freeze-thaw durability.
Main Methods:
- Proteins and denaturants were combined in solution to form complexes.
- Surface activity, foaming, flowability, and setting times were measured.
- Microstructure was analyzed using X-ray microcomputed tomography (Micro-CT) and scanning electron microscopy (SEM).
- Freeze-thaw resistance was evaluated through mass loss over 300 cycles.
Main Results:
- Certain protein-denaturant complexes showed significantly higher surface activity than individual components.
- Micro-CT revealed that specific complexes dramatically increased air-entrained porosity due to denaturation and synergistic effects.
- Proteins modified with lignin (Lig) and SDS, particularly Lys-Lig, Alb-Lig, Alb-SDS, and CP-Lig, showed the greatest improvements in air-entrained microstructure and freeze-thaw resistance.
- Some combinations were detrimental, reducing air-entrained porosity, indicating disruption of favorable protein conformations or interfacial incompatibility.
Conclusions:
- Controlled unfolding of proteins using denaturants can significantly enhance air-entraining performance and freeze-thaw durability of cement paste.
- The effectiveness of protein-denaturant complexes is highly specific to the protein and denaturant combination.
- Synergistic interactions at the bubble interface and protein conformational changes are critical factors influencing air void structure and cement durability.
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