Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein

Yungang Cao; Youling L. Xiong

doi:10.1016/j.foodchem.2015.02.036

Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein

Yungang Cao, Youling L. Xiong

Animal and Food Sciences

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

516 Scopus citations

Abstract

The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.

Original language	English
Pages (from-to)	235-243
Number of pages	9
Journal	Food Chemistry
Volume	180
DOIs	https://doi.org/10.1016/j.foodchem.2015.02.036
State	Published - Aug 1 2015

Bibliographical note

Publisher Copyright:
© 2015 Elsevier Ltd.

Keywords

Chlorogenic acid
Myofibrillar protein
Oxidation
Protein gelation
Rheology

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2015.02.036

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title = "Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein",

abstract = "The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.",

keywords = "Chlorogenic acid, Myofibrillar protein, Oxidation, Protein gelation, Rheology",

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

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AU - Cao, Yungang

AU - Xiong, Youling L.

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N2 - The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.

AB - The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.

KW - Chlorogenic acid

KW - Myofibrillar protein

KW - Oxidation

KW - Protein gelation

KW - Rheology

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JO - Food Chemistry

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Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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