食品科学

• 基础研究 • 上一篇    下一篇

微生物转谷氨酰胺酶诱导下鲢鱼糜凝胶的结构演化规律

郭秀瑾1,2,胡 杨1,2,尤 娟1,2,熊善柏1,2,*   

  1. 1.华中农业大学食品科学技术学院,湖北 武汉 430070;2.国家大宗淡水鱼加工技术研发分中心,湖北 武汉 430070
  • 出版日期:2016-03-15 发布日期:2016-03-17

Structural Evolution of MTGase-Induced Silver Carp Surimi Gels

GUO Xiujin1,2, HU Yang1,2, YOU Juan1,2, XIONG Shanbai1,2,*   

  1. 1. College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China;
    2. National R&D Branch Center for Conventional Freshwater Fish Processing (Wuhan), Wuhan 430070, China
  • Online:2016-03-15 Published:2016-03-17

摘要:

以鲢鱼糜为对象,通过检测微生物转谷氨酰胺酶(microbial transglutaminase,MTGase)诱导下不同凝胶化时间形成的鱼糜凝胶的质地特性、交联程度及网络微观结构,探讨鲢鱼糜凝胶的结构演化规律。力学特性结果表明,未添加MTGase(对照组)的鱼糜凝胶的破断力、凹陷深度、硬度、咀嚼性等随凝胶化时间延长显著增大(P<0.05),破断力在3~6 h达到平衡(约1 100 g),凹陷深度在1~2 h达到最大值(约17 mm),随着凝胶时间延长呈下降趋势;添加MTGase的鱼糜凝胶破断力在3 h时就达到最大值(P<0.05),硬度和咀嚼性随时间增加到3 h后趋于平衡,凹陷深度随时间延长逐渐降低(P<0.05)。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodiumdodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)结果显示,鲢鱼糜凝胶中肌球蛋白重链含量随凝胶化时间延长显著下降,添加MTGase组肌球蛋白重链含量明显低于对照组。两组鱼糜凝胶的网络孔隙当量直径均随凝胶化时间延长先减小后增大,在3 h时分别达到最致密的网络结构(P<0.05)。对照组和添加MTGase的鲢鱼糜凝胶分别在40 ℃凝胶化3~6 h或2~4 h时凝胶特性较好,通过凝胶化时间的调节可控制鱼糜凝胶的结构演化方向,获得高品质鱼糜制品。

关键词: 鱼糜凝胶, 微生物转谷氨酰胺酶, 结构演化, 微观结构, 交联程度

Abstract:

The texture, cross-linkage and microstructure of MTGase-induced silver carp surimi gels at various setting
times were measured to explore the pattern of structural evolution. The mechanical testing results showed that the breaking
force, deformation, hardness and chewiness of surimi gels without MTGase addition (control group) increased significantly
(P < 0.05) with extended setting time. The equilibrium breaking force (1 100 g) was achieved when the setting time was 3–6 h
and the highest deformation (17 mm) was obtained in non-MTGase group when the setting time was 1–2 h, followed by a
decrease with extended setting time. The highest breaking force, hardness and chewiness were obtained when the setting
time was extended up to 3 h in MTGase group, while the deformation decreased significantly (P < 0.05) with the extension
of setting time. SDS-PAGE results showed that myosin heavy chain (MHC) content decreased with the extension of
setting time and the MHC content of the MTGase group was lower than that of the control group. The pore size of surimi
gels decreased first and then increased significantly (P < 0.05), achieving the most compact network structure when the
setting time was 3 h. Better properties of surimi gels were obtained when the setting time was 3–6 h in the absence of
MTGase or 2–4 h in the presence of MTGase at 40 ℃. To conclude, structural evolution of surimi gels can be controlled by
adjusting the setting time to obtain high-quality surimi gel products.

Key words: surimi gel, microbial transglutaminase (MTGase), structure evolution, microstructure, cross-linkage

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