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Research Article | Open Access

Differential modulation of myofibrillar protein gelation by monophenolic acids with divergent sidechain groups

Anqi GuoAlma D. TrueYouling L. Xiong( )
Department of Animal and Food Sciences, University of Kentucky, Lexington, Kentucky 40546, USA
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Abstract

Six phenolic acids (PAs) with related structures, i.e., gallic acid (GA), syringic acid (SA), coumaric acid (CMA), caffeic acid (CFA), ferulic acid (FA), and chlorogenic acid (CA), were compared for their effects on the gelling properties of myofibrillar protein (MP) under oxidative conditions. Of the six PAs, only the smallest GA caused significant reductions of free amine and sulfhydryl content (by 26% and 7%, respectively, P < 0.05) and SA decreased protein carbonyl formation, while CA, the largest PA with an esterified quinic group, prevented oxidative loss of amines. All PAs quenched MP fluorescence with CA showing the highest efficacy (38% suppression). During thermal gelation, the GA-modified MP displayed the strongest myosin cross-linking. The elasticity (G′) and breaking strength of MP gels were markedly enhanced by the addition of PAs, and the final G′ value ranked in the order GA > CA > FA > CMA > SA > CFA, indicating complex roles of phenolic side groups.

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Food Science of Animal Products
Article number: 9240033
Cite this article:
Guo A, True AD, Xiong YL. Differential modulation of myofibrillar protein gelation by monophenolic acids with divergent sidechain groups. Food Science of Animal Products, 2023, 1(3): 9240033. https://doi.org/10.26599/FSAP.2023.9240033

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Received: 09 August 2023
Revised: 24 August 2023
Accepted: 18 September 2023
Published: 18 December 2023
© Beijing Academy of Food Sciences 2023.

Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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