Multidimensional mechanism of pulsed electric field synergized L-arginine upon goose meat tenderization: Based on molecular dynamics simulation and protein interaction network.

Rong Ma, Chen Chen, Zihang Shi, Yangyang Hu, Yangying Sun, Qiang Xia, Changyu Zhou, Daodong Pan

Abstract read

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Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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1 citing paper in PubMed.

Nutritional Regulation of Poultry Meat Quality: Research Progress from Phenotypic Improvement to Mechanism Elucidation.Foods (Basel, Switzerland) · 2026
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8 authors.

Rong MaNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Chen ChenNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Zihang ShiNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Yangyang HuNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Yangying SunNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Qiang XiaNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Changyu ZhouNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Daodong PanNational Key Laboratory of Quality and Safety of Agricultural Products, Ningbo University, Ningbo, Zhejiang 315211, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although pulsed electric field (PEF) and L-arginine alone can improve meat tenderness, their synergistic molecular mechanism remains unclear. This study first explored the tenderization mechanism of combined PEF and L-arginine (LP) in goose meat. Results showed that LP reduced goose meat shear force by 51.30%, with effects significantly superior to either treatment alone. Hematoxylin-eosin staining revealed that LP enlarged intermuscular spaces. Infrared spectroscopy indicated that LP induced a conformational shift from α-helix to β-sheet in myofibrillar proteins (MPs). Fluorescence spectroscopy showed a significantly increased fluorescence intensity, confirming structural unfolding of MPs. Enzyme activity assays showed that LP elevated calpain activity by 64.33%. SDS-PAGE further confirmed the accelerated degradation of troponin-T. Molecular dynamics simulations revealed that PEF primarily drives the restructuring of the enzyme-substrate binding interface, while L-arginine stabilizes the process by maintaining the hydrogen bond network. This study provides a theoretical basis for developing efficient and controllable meat tenderization technologies.

Indexed as

Endogenous enzymeL-arginineMolecular dockingProtein degradationPulsed electric fieldTenderness

Identifiers

PMID42006652

DOI10.1016/j.fochx.2026.103836

PMCPMC13091145

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.