Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties

Qingling Wang; Yan Jin; Youling L. Xiong

doi:10.1021/acs.jafc.8b03901

Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties

Qingling Wang, Yan Jin, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

93 Scopus citations

Abstract

Alkaline pH₁₂ shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) was remarkably improved (p < 0.05) with elevating the temperature and prolonging the holding time, reaching 97.5% at 80 °C for 60 min. The treated HPI exhibited a strong tendency of forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating was methodically controlled to 60 °C and 5 min, where the LAL content never exceeded 100 mg/100 g of protein and the loss of cysteine and lysine was also minimal. The emulsifying activity of HPI was improved by this mild pH shift-heating combination treatment as a result of the dissociation of protein subunits, unraveling of the tertiary structure, and exposure of hydrophobic groups. Moreover, the emulsion formed by the treated protein maintained a superior stability in particle size and distribution during storage.

Original language	English
Pages (from-to)	10827-10834
Number of pages	8
Journal	Journal of Agricultural and Food Chemistry
Volume	66
Issue number	41
DOIs	https://doi.org/10.1021/acs.jafc.8b03901
State	Published - Oct 17 2018

Bibliographical note

Funding Information:
*Telephone: 859-257-3822. Fax: 859-257-5318. E-mail: ylxiong@uky.edu. ORCID Youling L. Xiong: 0000-0002-2164-4783 Funding This work was supported by the United States Department of Agriculture (USDA) National Institute of Food and Agriculture (Hatch Project 2351267000) and an Oversea Study Fellowship from the China Scholarship Council (to Qingling Wang), approved for publication as journal article number 18-07-072 by the Director of the Kentucky Agricultural Experiment Station. Notes The authors declare no competing financial interest.

Publisher Copyright:
© Copyright 2018 American Chemical Society.

Keywords

amino acids
emulsifying activity
hemp seed protein isolate
lysinoalanine
solubility

ASJC Scopus subject areas

Chemistry (all)
Agricultural and Biological Sciences (all)

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10.1021/acs.jafc.8b03901

Cite this

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title = "Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties",

abstract = "Alkaline pH12 shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) was remarkably improved (p < 0.05) with elevating the temperature and prolonging the holding time, reaching 97.5% at 80 °C for 60 min. The treated HPI exhibited a strong tendency of forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating was methodically controlled to 60 °C and 5 min, where the LAL content never exceeded 100 mg/100 g of protein and the loss of cysteine and lysine was also minimal. The emulsifying activity of HPI was improved by this mild pH shift-heating combination treatment as a result of the dissociation of protein subunits, unraveling of the tertiary structure, and exposure of hydrophobic groups. Moreover, the emulsion formed by the treated protein maintained a superior stability in particle size and distribution during storage.",

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

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N1 - Funding Information: *Telephone: 859-257-3822. Fax: 859-257-5318. E-mail: ylxiong@uky.edu. ORCID Youling L. Xiong: 0000-0002-2164-4783 Funding This work was supported by the United States Department of Agriculture (USDA) National Institute of Food and Agriculture (Hatch Project 2351267000) and an Oversea Study Fellowship from the China Scholarship Council (to Qingling Wang), approved for publication as journal article number 18-07-072 by the Director of the Kentucky Agricultural Experiment Station. Notes The authors declare no competing financial interest. Publisher Copyright: © Copyright 2018 American Chemical Society.

PY - 2018/10/17

Y1 - 2018/10/17

N2 - Alkaline pH12 shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) was remarkably improved (p < 0.05) with elevating the temperature and prolonging the holding time, reaching 97.5% at 80 °C for 60 min. The treated HPI exhibited a strong tendency of forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating was methodically controlled to 60 °C and 5 min, where the LAL content never exceeded 100 mg/100 g of protein and the loss of cysteine and lysine was also minimal. The emulsifying activity of HPI was improved by this mild pH shift-heating combination treatment as a result of the dissociation of protein subunits, unraveling of the tertiary structure, and exposure of hydrophobic groups. Moreover, the emulsion formed by the treated protein maintained a superior stability in particle size and distribution during storage.

AB - Alkaline pH12 shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) was remarkably improved (p < 0.05) with elevating the temperature and prolonging the holding time, reaching 97.5% at 80 °C for 60 min. The treated HPI exhibited a strong tendency of forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating was methodically controlled to 60 °C and 5 min, where the LAL content never exceeded 100 mg/100 g of protein and the loss of cysteine and lysine was also minimal. The emulsifying activity of HPI was improved by this mild pH shift-heating combination treatment as a result of the dissociation of protein subunits, unraveling of the tertiary structure, and exposure of hydrophobic groups. Moreover, the emulsion formed by the treated protein maintained a superior stability in particle size and distribution during storage.

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Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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