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Nanostructure and functionality of enzymatically repolymerized whey protein hydrolysate
Amelia Chen1, Indra Tanidjaja1, Srinivasan Damodaran1
1Department of Food Science, University of Wisconsin-Madison, Madison, WI 53706, United States.
Food Chemistry
|April 3, 2018
Summary
Whey protein polymers were created and tested for foaming and emulsifying abilities. Different structures and charges affected their performance, with one type stabilizing foams and the other improving emulsion stability.
Area of Science:
- Food Science
- Protein Chemistry
- Materials Science
Background:
- Whey protein isolate (WPI) is a valuable food ingredient.
- Protein polymerization can modify functional properties.
- Enzymatic hydrolysis and polymerization offer tunable modification routes.
Purpose of the Study:
- To produce and characterize whey protein nanoparticles/polymers using transglutaminase (TGase) and thermolysin.
- To investigate the impact of polymerization and hydrolysis on protein structure.
- To evaluate the effect of these protein nanoparticles on foam and emulsion stability.
Main Methods:
- Whey proteins (WPI) were polymerized with TGase, with and without prior partial hydrolysis by thermolysin.
- Electrophoresis and Atomic Force Microscopy (AFM) were used for structural characterization.
- Foaming and emulsifying properties were assessed, along with emulsion storage stability.
Main Results:
- Polymerized WPI (WPI-TG) formed more stable foams compared to polymerized WPI hydrolysate (WPIH-TG).
- WPIH-TG yielded emulsions with superior stability over WPI-TG emulsions.
- Structural differences (size, charge) explained the varying performance in foams and emulsions.
Conclusions:
- Protein nanoparticles can impart Pickering stabilization to both foams and emulsions.
- Strong electrostatic repulsion between adsorbed nanoparticles destabilized foams but not emulsions.
- The specific structure and charge of protein polymers dictate their suitability for different food applications.
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