Expanded functionality of modified whey protein dispersions after transglutaminase catalysis

Area of Science:

• Food Science
• Biochemistry
• Protein Chemistry

Background:

• Modified whey protein concentrate (mWPC) is a key ingredient in food systems.
• Understanding protein cross-linking mechanisms is crucial for functional ingredient development.
• Enzymatic modification offers a targeted approach to alter protein functionality.

Purpose of the Study:

• To investigate the impact of microbial transglutaminase (TGase) cross-linking on mWPC functionality.
• To evaluate changes in gelation properties, thermal stability, and emulsion characteristics of TGase-modified mWPC.
• To assess the potential of TGase-mWPC as a high-performance ingredient.

Main Methods:

• Preparation of mWPC dispersions and cross-linking with TGase at pH 8.
• Real-time monitoring of gelation kinetics and determination of gelling temperatures.
• Measurement of gel strength, water holding capacity, and emulsion stability.
• Analysis of apparent viscosity and particle size of modified dispersions.

Main Results:

• TGase-mWPC dispersions gelled faster and at higher temperatures compared to controls.
• Prolonged TGase treatment increased gel strength but reduced it in TGase-mWPC compared to controls.
• Emulsions made with TGase-mWPC showed excellent stability and a 10-fold increase in viscosity.
• Particle size increased in covalently linked TGase-mWPC fractions.

Conclusions:

• TGase cross-linking significantly modifies mWPC functionality, enhancing gelation and thermal stability.
• TGase-treated mWPC improves emulsion stability and viscosity, indicating superior functional performance.
• Enzymatically modified mWPC offers a pathway to develop advanced ingredients for demanding food applications.