Mechanochemical unfolding facilitates protein-glutaminase deamidation and charge remodeling of myofibrillar protein to reduce low-salt-induced aggregation tendency
- 1Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, People's Republic of China
- 2College of Biology and Medicine, Chuzhou City Vocational College, Chuzhou, 239000, People's Republic of China
Abstract
Low-salt-induced aggregation tendency of myofibrillar protein (MP) reduces its solubility and functional performance under low ionic strength conditions. This study investigated whether high-pressure microfluidization(HPM)-induced mechanochemical unfolding could facilitate protein-glutaminase (PG) deamidation and charge remodeling of MP to reduce low-salt-induced aggregation tendency. MP dispersed under low-salt conditions (0.1 mol/L NaCl) was treated with HPM at 52, 69, 86 and 103 MPa, followed by PG deamidation, and its degree of deamidation, solubility, particle characteristics, surface charge, conformational changes, molecular interactions, and assembly morphology were analyzed. HPM disrupted the highly cross-linked MP structure and promoted conformational unfolding, thereby improving substrate accessibility for PG-mediated deamidation. Sequential HPM-PG treatment markedly improved low-salt MP dispersion with increased DD from 5.94% to 11.45% after HPM pretreatment, increasing solubility from 34.5% in untreated MP to 71.2–71.94% in MP-15000H-PG. This improvement was associated with a reduction in particle size, with MP-10000H-PG and MP-15000H-PG decreasing to 1408.67 and 1254.67 nm, respectively. Moreover, the ζ-potential shifted from −11.63 to −25.96 mV, indicating that PG-mediated conversion of glutamine (Gln) residues to glutamic acid (Glu) residues might have remodeled MP charge. Secondary structure, fluorescence, sulfhydryl, TEM, and asymmetrical flow field-flow fractionation analyses further showed that sequential treatment disrupted filamentous aggregates, exposed reactive groups, and prevented it from aggregating into coarse myofibrillar structures. These findings clarified that mechanochemical unfolding-assisted PG deamidation can convert low-salt-reassembled MP into a charge-stabilized dispersed state, providing a molecular strategy for developing highly soluble meat protein ingredients for salt-reduced food systems.
Related
- Glutaminase contributes to MYC-induced cell-autonomous autophagy and to RasV12-dependent non-autonomous autophagy in the Drosophila wing disc epithelium
- Study on the modulation of the properties of 3D printing pork mince and interaction mechanisms with myofibrillar proteins and fatty acids by gelatin.
- Exploring intermediates in mechanochemical cycle and mechanism of regulation of full-length Dynein
- Mechanochemical interactions dictate obstacle-induced cell turning by breaking symmetry in actin dynamics
- High-dimensional hippocampus representation facilitates learning of low-dimensional abstract representation and supports generalization
BibTeX
@article{yang2026mechanochemical,
title = {{Mechanochemical unfolding facilitates protein-glutaminase deamidation and charge remodeling of myofibrillar protein to reduce low-salt-induced aggregation tendency}},
author = {Ningle Yang and Yating Liu and Xin Chen and Zongyun Yang and Zhen Li and Yating Xiong and Xinglian Xu and Peng Wang},
journal = {Current Research in Food Science},
year = {2026},
month = oct,
doi = {10.1016/j.crfs.2026.101606},
url = {https://doi.org/10.1016/j.crfs.2026.101606},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - Mechanochemical unfolding facilitates protein-glutaminase deamidation and charge remodeling of myofibrillar protein to reduce low-salt-induced aggregation tendency
AU - Ningle Yang
AU - Yating Liu
AU - Xin Chen
AU - Zongyun Yang
AU - Zhen Li
AU - Yating Xiong
AU - Xinglian Xu
AU - Peng Wang
PY - 2026
DA - 2026/10/23
JO - Current Research in Food Science
DO - 10.1016/j.crfs.2026.101606
UR - https://doi.org/10.1016/j.crfs.2026.101606
AB - Low-salt-induced aggregation tendency of myofibrillar protein (MP) reduces its solubility and functional performance under low ionic strength conditions. This study investigated whether high-pressure microfluidization(HPM)-induced mechanochemical unfolding could facilitate protein-glutaminase (PG) deamidation and charge remodeling of MP to reduce low-salt-induced aggregation tendency. MP dispersed under low-salt conditions (0.1 mol/L NaCl) was treated with HPM at 52, 69, 86 and 103 MPa, followed by PG deamidation, and its degree of deamidation, solubility, particle characteristics, surface charge, conformational changes, molecular interactions, and assembly morphology were analyzed. HPM disrupted the highly cross-linked MP structure and promoted conformational unfolding, thereby improving substrate accessibility for PG-mediated deamidation. Sequential HPM-PG treatment markedly improved low-salt MP dispersion with increased DD from 5.94% to 11.45% after HPM pretreatment, increasing solubility from 34.5% in untreated MP to 71.2–71.94% in MP-15000H-PG. This improvement was associated with a reduction in particle size, with MP-10000H-PG and MP-15000H-PG decreasing to 1408.67 and 1254.67 nm, respectively. Moreover, the ζ-potential shifted from −11.63 to −25.96 mV, indicating that PG-mediated conversion of glutamine (Gln) residues to glutamic acid (Glu) residues might have remodeled MP charge. Secondary structure, fluorescence, sulfhydryl, TEM, and asymmetrical flow field-flow fractionation analyses further showed that sequential treatment disrupted filamentous aggregates, exposed reactive groups, and prevented it from aggregating into coarse myofibrillar structures. These findings clarified that mechanochemical unfolding-assisted PG deamidation can convert low-salt-reassembled MP into a charge-stabilized dispersed state, providing a molecular strategy for developing highly soluble meat protein ingredients for salt-reduced food systems.
SN - 2665-9271
ER -