Most plant storage proteins are of a compact structure comprised of multiple subunits largely via hydrophobic patches and electrostatic attractions. Such structural complexity hinders the solubility and functional behavior of proteins for use as food ingredients. When exposed to extreme pH conditions that promote charge repulsions followed by neutralization, the quaternary structure is disrupted and individual monomers obtain a molten state. The process, known as pH shift, can produce highly soluble protein monomers and aggregates with excellent emulsifying and foaming properties due to redistributions of surface-active amino acid side chain groups. This brief review presents conceptual as well as latest industry-relevant research in the field that projects promise and potential of this technology.
|Number of pages||7|
|Journal||Current Opinion in Food Science|
|State||Published - Feb 2018|
Bibliographical noteFunding Information:
This study was supported by the USDA National Institute of Food and Agriculture (USA) (Hatch project 1005724 ) and the National Natural Science Foundation, China (Grant No. 31301497 ). Approved for publication as journal article number 17-07-110 by the Director of the Kentucky Agricultural Experiment Station.
© 2018 Elsevier Ltd
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology