Partial removal of phenolics coupled with alkaline ph shift improves canola protein interfacial properties and emulsion in in vitro digestibility

Jiang Jiang; Yunqing Nie; Xuemei Sun; Youling L. Xiong

doi:10.3390/foods10061283

Partial removal of phenolics coupled with alkaline ph shift improves canola protein interfacial properties and emulsion in in vitro digestibility

Jiang Jiang, Yunqing Nie, Xuemei Sun, Youling L. Xiong

Animal and Food Sciences

Producción científica: Article › revisión exhaustiva

19 Citas (Scopus)

Resumen

The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH₁₂ shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53% of phenolics were removed from the CPI after the extraction with 70% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH₁₂ shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion.

Idioma original	English
Número de artículo	1283
Publicación	Foods
Volumen	10
N.º	6
DOI	https://doi.org/10.3390/foods10061283
Estado	Published - jun 2021

Nota bibliográfica

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Financiación

Funding: This study was supported by the National Key Research and Development Program of China (Grant No. 2016YFD0401404). The joint effort was also supported by the USDA National Institute of Food and Agriculture of the USA (Hatch Project 1020736). This study was supported by the National Key Research and Development Program of China (Grant No. 2016YFD0401404). The joint effort was also supported by the USDA National Institute of Food and Agriculture of the USA (Hatch Project 1020736). Authors are grateful for the technical support of the university research core facilities at Jiangnan University.

Financiadores	Número del financiador
USDA National Institute of Food and Agriculture of the USA	1020736
Jiangnan University
National Key Basic Research and Development Program of China	2016YFD0401404

ASJC Scopus subject areas

Food Science
Microbiology
Health(social science)
Health Professions (miscellaneous)
Plant Science

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@article{e0093a098410467abceedd1bfaf7ee9c,

title = "Partial removal of phenolics coupled with alkaline ph shift improves canola protein interfacial properties and emulsion in in vitro digestibility",

abstract = "The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH12 shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53\% of phenolics were removed from the CPI after the extraction with 70\% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH12 shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion.",

keywords = "Canola protein isolate, Dephenol, Emulsifying properties, In vitro digestion, PH shift, Solubility",

author = "Jiang Jiang and Yunqing Nie and Xuemei Sun and Xiong, \{Youling L.\}",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2021",

month = jun,

doi = "10.3390/foods10061283",

language = "English",

volume = "10",

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TY - JOUR

T1 - Partial removal of phenolics coupled with alkaline ph shift improves canola protein interfacial properties and emulsion in in vitro digestibility

AU - Jiang, Jiang

AU - Nie, Yunqing

AU - Sun, Xuemei

AU - Xiong, Youling L.

PY - 2021/6

Y1 - 2021/6

N2 - The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH12 shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53% of phenolics were removed from the CPI after the extraction with 70% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH12 shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion.

AB - The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH12 shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53% of phenolics were removed from the CPI after the extraction with 70% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH12 shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion.

KW - Canola protein isolate

KW - Dephenol

KW - Emulsifying properties

KW - In vitro digestion

KW - PH shift

KW - Solubility

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M3 - Article

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SN - 2304-8158

VL - 10

JO - Foods

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Partial removal of phenolics coupled with alkaline ph shift improves canola protein interfacial properties and emulsion in in vitro digestibility

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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