2021
DOI: 10.1021/acs.jafc.0c04365
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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… Show more

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Cited by 67 publications
(48 citation statements)
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References 44 publications
(87 reference statements)
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“…One is via quinones acting as a bridge to connect two peptides (protein-quinoneprotein) and the other is the oxidative transformation of sulfhydryls to disulfide bonds. 32 Han et al 27 also suggested that the molar masses of scallop gonad protein isolates and its EGCG conjugates were 101.3 and 225.3 kDa, respectvely. Liu et al 33 reported that, after conjugation with EGCG, the molar mass of zein increased from 36.0 to 54.7 kDa.…”
Section: Resultsmentioning
confidence: 99%
“…One is via quinones acting as a bridge to connect two peptides (protein-quinoneprotein) and the other is the oxidative transformation of sulfhydryls to disulfide bonds. 32 Han et al 27 also suggested that the molar masses of scallop gonad protein isolates and its EGCG conjugates were 101.3 and 225.3 kDa, respectvely. Liu et al 33 reported that, after conjugation with EGCG, the molar mass of zein increased from 36.0 to 54.7 kDa.…”
Section: Resultsmentioning
confidence: 99%
“…According to these results, it is possible that some phenolic compounds could be extracted under the conditions used for the protein SP extraction, influencing the physicochemical properties, including the gel-like structure, of MP in SP through both covalent and noncovalent interactions (reversible or irreversible pathways) resulting in the blockage of exposed hydrophobic sites, reducing the surface area, lowering the concentration of MP available to interact in the formation of the gel-like structure and affecting the texture properties. In addition, the lack of improvement on the texture properties in treatments where PUP extract was used may be attributed to the increase in free SH groups content, and their prompt to be attacked by the phenol ring structure (quinone) forming protein−quinone complexes, altering the gelation capability of proteins, which is the most important texture property in meat products ( Guo et al, 2021 ).…”
Section: Resultsmentioning
confidence: 99%
“…MPE with concentration higher than 0.1% had higher expressible drip than that with 0.01% ( p < 0.05), which may be linked to the net results of protein and lipid oxidation as well as the degree of gelation and the emulsifying ability of the MPE at different concentrations. Guo et al [ 57 ] reported that phenolic compounds such as gallic acid, chlorogenic acid, propyl gallate, quercetin, catechin, and (−)-epigallocatechin-3-gallate (EGCG) caused unfolding and promoted cross-linking of myofibrillar proteins in myofibrillar protein–emulsion composite gel. All phenolics retarded the lipid oxidation of gel upon refrigerated storage [ 57 ].…”
Section: Resultsmentioning
confidence: 99%
“…Guo et al [ 57 ] reported that phenolic compounds such as gallic acid, chlorogenic acid, propyl gallate, quercetin, catechin, and (−)-epigallocatechin-3-gallate (EGCG) caused unfolding and promoted cross-linking of myofibrillar proteins in myofibrillar protein–emulsion composite gel. All phenolics retarded the lipid oxidation of gel upon refrigerated storage [ 57 ].…”
Section: Resultsmentioning
confidence: 99%