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 degrees 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 a-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.