Modification of myofibrillar protein via glycation: Physicochemical characterization, rheological behavior and solubility property

Functionalities of muscle protein are vital in the qualitative characteristics of final products. Glycation was explored as a promising way for upgrading the functionalities of muscle protein. Myofibrillar protein (MP) was conjugated with dextran (DX) in a liquid solution at a moderate temperature (37 °C). The conjugation was verified by UV–Vis spectrometry and electrophoresis analysis. The results suggested that glycation affected the particle size and morphology of MP, and glycation induced unfolding of the MP and loss of α-helix structures. As the molecular weight of DX was increased, the glycated MP displayed shear-thinning behavior with better flow ability and higher solubility, and the solubility at isoelectric point was noticeably improved (P < 0.05). The thermal gelling ability seemed to be impaired, probably because glycation exerted a protective effect on MP by inhibiting aggregation during heat-induced gelation. The results provide a further understanding of the relationship between the structure and functionalities of glycated MP, which can be utilized as a new additive.