即食重组纤维感鱼糜制品的制备及特性表征

Preparation and characterizations of ready-to-eat reconstructed fiber surimi products

以鱼糜和风干鸡胸肉粒为原料,通过控制食盐、水分和谷氨酰胺转胺酶(transglutaminase,TGase)添加量,采用响应面分析法优化制备了一种具有纤维感的即食重组鱼糜制品,并以微观结构、内源荧光光谱、聚丙烯酰胺凝胶电泳以及化学作用力等指标表征复合鱼糜制品的热稳定特性。结果表明,食盐添加量0.5%、水分添加量4.1%、TGase添加量0.5%条件下制备的重组鱼糜制品经高温灭菌后仍具有较高的咀嚼度(2812.8),且高温灭菌前后咀嚼度降低率仅为5.7%。一定程度的高温处理导致肌原纤维蛋白活性基团暴露,促使其发生聚集和交联,形成有序的网状结构。但随着处理温度的进一步升高,凝胶网络结构松散,孔洞变大,肌纤维断裂明显。SDS-PAGE结果表明,随着处理温度的升高,肌球蛋白重链发生明显降解。化学作用力分析结果表明,疏水相互作用和二硫键为维持蛋白质热稳定的主要作用力。该研究可为丰富鱼糜制品种类,开发一种即食鱼糜制品提供参考。

In this study,the optimal parameters of ready-to-eat reconstructed fiber surimi products were obtained by response surface methodology,and the thermal stabilization mechanisms were further emphasized by SDS-PAGE,fluorescence spectra,chemical force analysis and microstructure observation(SEM and HE staining).A high chewiness value(2812.8)was found for reconstructed fiber surimi products formulated with 0.5%salt,4.1%water and 5.7%TGase after thermal treatments.The given heating treatment induced the exploration of active groups of myofibrillar proteins and the subsequent aggregation,which was responsible for the formation of the well-order microstructure.However,the increasing temperature disrupted the homogeneous network,leading to was obvious fiber fracture.Meanwhiles,with the increase in the treatment temperature,the MHC was significantly degraded,and the thermal stability of actin was better.The high resistance to thermal degradation was supported by hydrophobic interactions and disulfide covalent bonds.This work can provide some references to the development of ready-to-eat reconstructed surimi products.