Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds

Anqi Guo; Jiang Jiang; Alma D. True; Youling L. Xiong

doi:10.1021/acs.jafc.0c04365

Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds

Anqi Guo
, Jiang Jiang
, Alma D. True
, Youling L. Xiong

Animal and Food Sciences

Producción científica: Article › revisión exhaustiva

125 Citas (Scopus)

Resumen

Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.

Idioma original	English
Páginas (desde-hasta)	1308-1317
Número de páginas	10
Publicación	Journal of Agricultural and Food Chemistry
Volumen	69
N.º	4
DOI	https://doi.org/10.1021/acs.jafc.0c04365
Estado	Published - feb 3 2021

Nota bibliográfica

Publisher Copyright:
© 2021 American Chemical Society.

Financiación

This work was supported by the USDA National Institute of Food and Agriculture, Hatch project 1020736. This research was supported by the Biospecimen Procurement & Translational Pathology Shared Resource Facility of the University of Kentucky Markey Cancer Center (P30CA177558).

Financiadores	Número del financiador
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative	1020736
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative
University of Kentucky Markey Cancer Center	P30CA177558
University of Kentucky Markey Cancer Center

ASJC Scopus subject areas

General Chemistry
General Agricultural and Biological Sciences

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10.1021/acs.jafc.0c04365

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title = "Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds",

abstract = "Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.",

keywords = "gelation, glucose oxidase, myofibrillar protein, phenolics, protein and lipid oxidation",

author = "Anqi Guo and Jiang Jiang and True, \{Alma D.\} and Xiong, \{Youling L.\}",

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AU - Guo, Anqi

AU - Jiang, Jiang

AU - True, Alma D.

AU - Xiong, Youling L.

PY - 2021/2/3

Y1 - 2021/2/3

N2 - Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.

AB - Protein gelation is an important phenomenon in processed meats. The present study investigated the structure-activity relationship of six phenolic compounds, that is, gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) in a myofibrillar protein (MP) gelling system under controlled oxidative conditions. All phenolics induced unfolding and promoted cross-linking of MP via sulfhydryl or amine groups. At an equal molar concentration, EGCG boosted the elastic MP gel network more than other phenolics except PG. However, all three monophenols (GA, CA, and PG) and the diphenol QT increased the MP gel strength more than CC (diphenol) and EGCG (triphenol). The flavanol structure appeared to interfere with the protein gel structure development. All phenolics retarded lipid oxidation in MP-emulsion composite gels during refrigerated storage with the least polar phenolic compounds, PG and QT, showing the greatest efficacy.

KW - gelation

KW - glucose oxidase

KW - myofibrillar protein

KW - phenolics

KW - protein and lipid oxidation

UR - https://www.scopus.com/pages/publications/85100726892

UR - https://www.scopus.com/pages/publications/85100726892#tab=citedBy

U2 - 10.1021/acs.jafc.0c04365

DO - 10.1021/acs.jafc.0c04365

M3 - Article

C2 - 33494593

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SN - 0021-8561

VL - 69

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EP - 1317

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 4

ER -

Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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Huella

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