# Preliminary Exploration on the Regulatory Mechanism of Ionic Strength on Conformation and Hydration of Silver Carp Myosin

**Authors:** Kaiqi Li, Ramy M. Khoder, Yanlei Gao, Juan You, Tao Yin, Ru Liu

PMC · DOI: 10.3390/foods14101790 · Foods · 2025-05-18

## TL;DR

This study explores how salt concentration affects the structure and solubility of myosin in silver carp muscle, improving gel quality in fish products.

## Contribution

The novel contribution is identifying how ionic strength influences myosin conformation and hydration through experimental and simulation methods.

## Key findings

- Proper ionic strength (0.3–0.8 mol/L) significantly improves myosin solubility and reduces protein size.
- Increased ionic strength extends myosin structure and enhances protein–water interactions via hydrogen bonds.
- Molecular dynamics simulations confirm the role of ionic strength in increasing hydrogen bonds between myosin and water.

## Abstract

Myosin is abundant in fish muscle tissue and plays a crucial role in gel quality of fish products. The gel forming ability of myosin is related to its solubility and conformation in ionic solution. This study investigated the regulation of NaCl concentrations (0.0~1.0 mol/L) on the solubility of silver carp (Hypophthalmichthys molitrix) myosin from the perspectives of conformation and hydration behavior. Results revealed that proper ionic strength (0.3~0.8 mol/L) significantly improved the solubility of myosin and reduced the average protein size (p < 0.05). Atomic force microscopy (AFM) observation also confirmed a decrease in the size of myosin aggregates. Increasing ionic strength induced the extending of the myosin structure and exposure of aromatic residues. These conformational changes enhanced protein–water interactions through hydrogen bonds, manifested as the formation of hydration layers. Molecular dynamics (MD) simulations also confirmed that appropriate ionic strength increased the number of hydrogen bonds between myosin and water molecules. In conclusion, proper ionic strength (0.3~0.8 mol/L)-induced exposure of polar groups in myosin enhances its hydration capacity, thereby improving solubility.

## Linked entities

- **Proteins:** MYH14 (myosin heavy chain 14)
- **Species:** Hypophthalmichthys molitrix (taxon 13095)

## Full-text entities

- **Chemicals:** NaCl (MESH:D012965), water (MESH:D014867), hydrogen (MESH:D006859)
- **Species:** Hypophthalmichthys molitrix (silver carp, species) [taxon 13095]

## Full text

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## Figures

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## References

67 references — full list in the complete paper: https://tomesphere.com/paper/PMC12111596/full.md

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Source: https://tomesphere.com/paper/PMC12111596