Mechanochemical unfolding facilitates protein-glutaminase deamidation and charge remodeling of myofibrillar protein to reduce low-salt-induced aggregation tendency
- DOI
- 10.1016/j.crfs.2026.101606
- Published
- 2026
- Container
- Current Research in Food Science
- Publisher
- Elsevier BV
- Open access
- unknown
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Cite this work
BibTeX
@article{allodium:10.1016/j.crfs.2026.101606,
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},
year = {2026},
journal = {Current Research in Food Science},
doi = {10.1016/j.crfs.2026.101606},
url = {https://doi.org/10.1016/j.crfs.2026.101606}
}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 JO - Current Research in Food Science DO - 10.1016/j.crfs.2026.101606 UR - https://doi.org/10.1016/j.crfs.2026.101606 ER -
APA
Yang, N., Liu, Y., Chen, X., Yang, Z., Li, Z., Xiong, Y., Xu, X., & Wang, P. (2026). Mechanochemical unfolding facilitates protein-glutaminase deamidation and charge remodeling of myofibrillar protein to reduce low-salt-induced aggregation tendency. Current Research in Food Science. https://doi.org/10.1016/j.crfs.2026.101606
Source records
- crossref · retrieved 2026-11-08T06:17:40.500Z