Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests

Yanyun Cao; Youling L. Xiong

doi:10.1021/acs.jafc.7b03006

Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests

Yanyun Cao
, Youling L. Xiong

Animal and Food Sciences

Producción científica: Article › revisión exhaustiva

52 Citas (Scopus)

Resumen

Preheated (80 °C for 9 min) whey protein isolate (HWPI) was reacted with 20, 120, and 240 μmol/g (protein basis) gallic acid (GA) or epigallocatechin gallate (EGCG) at neutral pH and 25 °C. Isothermal titration calorimetry and fluorometry showed a similar trend that GA binding to HWPI was moderate but weaker than EGCG binding. However, the shift of maximal fluorescence emission wavelength in opposite directions in response to GA (blue) and EGCG (red) suggests discrepant binding patterns. Electrophoresis results showed that EGCG induced formation of HWPI complexes while GA only had a marginal effect. Both free and phenolic-bound HWPI exhibited mild antiradical activity. However, when subjected to in vitro digestion, synergistic radical-scavenging activity was produced between the phenolics and peptides with the highest synergism being observed on 120 μmol/g phenolics.

Idioma original	English
Páginas (desde-hasta)	8443-8450
Número de páginas	8
Publicación	Journal of Agricultural and Food Chemistry
Volumen	65
N.º	38
DOI	https://doi.org/10.1021/acs.jafc.7b03006
Estado	Published - sept 27 2017

Nota bibliográfica

Publisher Copyright:
© 2017 American Chemical Society.

Financiación

Article number 17-07-059 approved for publication by the Director of the Kentucky Agricultural Experiment Station. This research was supported by the USDA National Institute of Food and Agriculture (Hatch Project 1005724) and an Oversea Study Fellowship from the China Scholarship Council (to Y.C.). Notes The authors declare no competing financial interest.

Financiadores	Número del financiador
National Institute of Food and Agriculture	1005724
China Scholarship Council

ASJC Scopus subject areas

General Chemistry
General Agricultural and Biological Sciences

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title = "Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests",

abstract = "Preheated (80 °C for 9 min) whey protein isolate (HWPI) was reacted with 20, 120, and 240 μmol/g (protein basis) gallic acid (GA) or epigallocatechin gallate (EGCG) at neutral pH and 25 °C. Isothermal titration calorimetry and fluorometry showed a similar trend that GA binding to HWPI was moderate but weaker than EGCG binding. However, the shift of maximal fluorescence emission wavelength in opposite directions in response to GA (blue) and EGCG (red) suggests discrepant binding patterns. Electrophoresis results showed that EGCG induced formation of HWPI complexes while GA only had a marginal effect. Both free and phenolic-bound HWPI exhibited mild antiradical activity. However, when subjected to in vitro digestion, synergistic radical-scavenging activity was produced between the phenolics and peptides with the highest synergism being observed on 120 μmol/g phenolics.",

keywords = "binding, heat-unfolded whey protein isolate, in vitro digestion, phenolic derivative, synergistic radical scavenging activity",

author = "Yanyun Cao and Xiong, \{Youling L.\}",

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doi = "10.1021/acs.jafc.7b03006",

language = "English",

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AU - Cao, Yanyun

AU - Xiong, Youling L.

PY - 2017/9/27

Y1 - 2017/9/27

N2 - Preheated (80 °C for 9 min) whey protein isolate (HWPI) was reacted with 20, 120, and 240 μmol/g (protein basis) gallic acid (GA) or epigallocatechin gallate (EGCG) at neutral pH and 25 °C. Isothermal titration calorimetry and fluorometry showed a similar trend that GA binding to HWPI was moderate but weaker than EGCG binding. However, the shift of maximal fluorescence emission wavelength in opposite directions in response to GA (blue) and EGCG (red) suggests discrepant binding patterns. Electrophoresis results showed that EGCG induced formation of HWPI complexes while GA only had a marginal effect. Both free and phenolic-bound HWPI exhibited mild antiradical activity. However, when subjected to in vitro digestion, synergistic radical-scavenging activity was produced between the phenolics and peptides with the highest synergism being observed on 120 μmol/g phenolics.

AB - Preheated (80 °C for 9 min) whey protein isolate (HWPI) was reacted with 20, 120, and 240 μmol/g (protein basis) gallic acid (GA) or epigallocatechin gallate (EGCG) at neutral pH and 25 °C. Isothermal titration calorimetry and fluorometry showed a similar trend that GA binding to HWPI was moderate but weaker than EGCG binding. However, the shift of maximal fluorescence emission wavelength in opposite directions in response to GA (blue) and EGCG (red) suggests discrepant binding patterns. Electrophoresis results showed that EGCG induced formation of HWPI complexes while GA only had a marginal effect. Both free and phenolic-bound HWPI exhibited mild antiradical activity. However, when subjected to in vitro digestion, synergistic radical-scavenging activity was produced between the phenolics and peptides with the highest synergism being observed on 120 μmol/g phenolics.

KW - binding

KW - heat-unfolded whey protein isolate

KW - in vitro digestion

KW - phenolic derivative

KW - synergistic radical scavenging activity

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ER -

Binding of Gallic Acid and Epigallocatechin Gallate to Heat-Unfolded Whey Proteins at Neutral pH Alters Radical Scavenging Activity of in Vitro Protein Digests

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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