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Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates
Lee Cadesky1, Markus Walkling-Ribeiro1, Kyle T Kriner1
1Department of Food Science, Cornell University, Ithaca, NY 14853.
Journal of Dairy Science
|June 26, 2017
Summary
High-pressure processing alters milk proteins, causing casein micelle changes and serum protein denaturation. This research explores novel food textures from these modified milk protein systems.
Area of Science:
- Food Science and Technology
- Protein Chemistry
- Dairy Science
Background:
- Milk protein concentrates (MPC) and micellar casein concentrates (MCC) are vital in food formulation.
- Understanding high-pressure processing (HPP) effects on these proteins is crucial for developing new food products.
Purpose of the Study:
- To investigate the structural and physicochemical changes in MPC and MCC induced by HPP.
- To explore the potential of HPP for creating novel milk protein-based food textures.
Main Methods:
- High-pressure processing (150-450 MPa) of 2.5% and 10% (wt/vol) protein solutions.
- Analysis using dynamic light scattering, rheology, FTIR spectroscopy, SEM, proteomics, and mineral analysis.
Main Results:
- HPP induced casein micelle structural changes and serum protein denaturation.
- Soluble calcium-binding caseins increased; soluble calcium and phosphorus levels varied with pressure.
- 450 MPa treatment formed weak physical gels with casein substructures (15-20 nm).
Conclusions:
- HPP destabilizes casein micelles and denatures serum proteins, with effects dependent on pressure and protein concentration.
- HPP offers a method to create unique textures in milk protein systems, potentially enhancing nutritional quality.
Keywords:
high-pressure processingmicellar casein concentratemilk protein concentratepressure-induced milk protein gelMore Related Videos
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