Thermo-reversible gelation and enhanced umami perception of myofibrillar proteins induced by protein-glutaminase-mediated deamidation

Weijun Leng; Ying Li; Xin Liang; Li Yuan; Xiuting Li; Ruichang Gao

doi:10.1016/j.foodchem.2025.142802

Thermo-reversible gelation and enhanced umami perception of myofibrillar proteins induced by protein-glutaminase-mediated deamidation

Food Chem. 2025 Jan 6:471:142802. doi: 10.1016/j.foodchem.2025.142802. Online ahead of print.

Authors

Weijun Leng¹, Ying Li², Xin Liang³, Li Yuan⁴, Xiuting Li⁵, Ruichang Gao⁶

Affiliations

¹ School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China.
² School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
³ Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China.
⁴ School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
⁵ Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China. Electronic address: [email protected].
⁶ School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China. Electronic address: [email protected].

PMID: 39793361
DOI: 10.1016/j.foodchem.2025.142802

Abstract

In this study, the absolute electrostatic charge of myofibrillar protein (MP) was substantially increased by protein-glutaminase (PG) treatment, which was a critical step for achieving the dissociation and solubility of MP under low salt condition. The PG-treated MP exhibited the capacity to form thermo-reversible gels that could be melted through heating and subsequently reformed into a stable gel structure upon refrigeration. The results of SDS-PAGE further revealed that the levels of soluble monomeric myosin and actin in the supernatant of deamidated MP (DMP) gels were markedly elevated, and confirmed the increased formation of intermolecular disulfide bond between myosin and actin. Additionally, moderate deamidation was beneficial for the improvements of MP gel properties, especially in terms of water-holding capacity and springiness. Electronic tongue and correlation analysis indicated that the umami perception of DMP was significantly enhanced because of the conversion of glutamine (Gln) to glutamate (Glu) residues that induced by PG deamidation.

Keywords: Gel; Low-salt; Myofibrillar protein; Protein-glutaminase; Thermo-reversibility; Umami perception.