Abstract:

Transglutaminase catalyses the cross-linking of myofibrillar proteins. Textural properties of surimi gel can
be transformed from elastico-viscous body to elastico-crisp body in response to an increase in cross-linking degree,
accompanied by an obvious change in its flavor. The flavor diffusion and release are closely related to the degree of
compactness and interactions of gel structure. So it is very meaningful to study the relationship between the cross-linking
degree and texture properties of foods, and the diffusion behavior of flavor compounds in gel networks. In this paper, the
mechanism of transglutaminase-catalyzed cross-linking of myofibrillar protein is summarized. Existing assay methods for
the cross-linking of myofibrillar protein and its influencing factors are also reviewed. The effects of cross-linking degree on
surimi gelation and flavor are discussed. Moreover, further research directions are proposed.

Key words: transglutaminase, myofibrillar proteins, cross-linking degree, assay methods, surimi gelation, influencing factors