肌原纤维蛋白转谷氨酰胺酶交联程度对鱼糜凝胶及其风味释放影响的研究进展

Effect of Transglutaminase-Catalyzed Cross-Linking Degree of Myofibrillar Protein on Surimi Gelation and Flavor Release

转谷氨酰胺酶可以催化肌原纤维蛋白发生交联反应。随着交联程度的增加,鱼糜凝胶从弹黏体变为弹脆体,风味也随之改变。风味物质的扩散、释放与凝胶网络的交联程度密切相关,因此深入了解交联程度与食品品质的关系及风味物质在凝胶网络中的扩散行为显得尤为重要。本文总结转谷氨酰胺酶催化肌原纤维蛋白的交联机理,归纳了国内外对肌原纤维蛋白交联程郭彩霞度的测定方法与影响因素,探讨交联程度对鱼糜蛋白的凝胶特性与风味释放的影响,并对今后的研究方向提出思考与展望。

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.