A pH shift approach to the improvement of interfacial properties of plant seed proteins

Jiang Jiang; Qingling Wang; Youling L. Xiong

doi:10.1016/j.cofs.2018.01.002

A pH shift approach to the improvement of interfacial properties of plant seed proteins

Jiang Jiang, Qingling Wang, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Review article › peer-review

107 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	50-56
Number of pages	7
Journal	Current Opinion in Food Science
Volume	19
DOIs	https://doi.org/10.1016/j.cofs.2018.01.002
State	Published - Feb 2018

Bibliographical note

Funding 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.

Publisher Copyright:
© 2018 Elsevier Ltd

ASJC Scopus subject areas

Food Science
Applied Microbiology and Biotechnology

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10.1016/j.cofs.2018.01.002

Cite this

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abstract = "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.",

author = "Jiang Jiang and Qingling Wang and Xiong, {Youling L.}",

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AU - Jiang, Jiang

AU - Wang, Qingling

AU - Xiong, Youling L.

N1 - Funding 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. Publisher Copyright: © 2018 Elsevier Ltd

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N2 - 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.

AB - 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.

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A pH shift approach to the improvement of interfacial properties of plant seed proteins

Abstract

Bibliographical note

ASJC Scopus subject areas

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