College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China; Collaborative Innovation Center for Efficient and Health Production of Fisheries in Hunan Province, Changde, Hunan 415000, PR China.
College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China; Collaborative Innovation Center for Efficient and Health Production of Fisheries in Hunan Province, Changde, Hunan 415000, PR China; National R&D Branch Center for Conventional Freshwater Fish Processing (Wuhan), Wuhan, Hubei 430070, PR China.
Food Chem. 2018 Apr 15;245:557-563. doi: 10.1016/j.foodchem.2017.10.139. Epub 2017 Oct 31.
Physicochemical and gelation properties of myofibrillar proteins from silver carp surimi as affected by chopping under different vacuum degrees (0, 0.01, 0.02, 0.04, 0.06 and 0.08 MPa) were investigated. With the increase of vacuum degree, size and quantity of air bubbles in surimi paste decreased, disulfide bond content of myofibrillar proteins decreased significantly (p < .05) and then slight increased (p > .05), while surface hydrophobicity of myofibrillar proteins increased gradually (p < .05). Gel mechanical properties, chemical interactions (nonspecific associations, hydrogen bond and hydrophobic interactions) and FAXL (cross-linking degree of free amino group) of heat-induced surimi gel increased significantly (p < .05) with vacuum degree. Scanning electron microscopy (SEM) observation showed that three-dimensional network of surimi gel under higher vacuum degree was more compact and orderly. Results indicated that vacuum chopping imparted physicochemical and structural changes of fish myofibrillar protein, which might contribute to the improvement in gelling properties of myofibrillar proteins.
研究了不同真空度（0、0.01、0.02、0.04、0.06 和 0.08 MPa）下斩拌对鲢鱼鱼糜肌原纤维蛋白理化性质和凝胶性能的影响。随着真空度的增加，鱼糜糊中气泡的大小和数量减少，肌原纤维蛋白中二硫键含量显著降低（p <.05），然后略有增加（p >.05），而肌原纤维蛋白表面疏水性逐渐增加（p <.05）。随着真空度的增加，热诱导鱼糜凝胶的凝胶机械性能、化学相互作用（非特异性结合、氢键和疏水相互作用）和 FAXL（游离氨基交联度）显著增加（p <.05）。扫描电子显微镜（SEM）观察表明，在较高真空度下，鱼糜凝胶的三维网络更加紧密有序。结果表明，真空斩拌赋予了鱼肌原纤维蛋白理化性质和结构的变化，这可能有助于改善肌原纤维蛋白的凝胶性能。
