以浙东大白鹅为原料，拉曼光谱技术为主要分析手段，研究白酒体积分数对浙东白鹅胸脯肉肌原纤维蛋白结构的影响。结果显示，随着白酒体积分数的增大，肌原纤维蛋白溶解度增大（p<0.05），表面疏水性降低（p<0.05）。在白酒体积分数较低时形成的凝胶特性较好，其微观结构很均匀，随着白酒体积分数的进一步增大，凝胶网络孔径变大，蛋白凝胶保水性显著降低(p<0.05)。随着白酒体积分数的增大，二硫键的三种构象之间发生了转变；对照组中酰胺Ⅰ带的主峰出现在1655 cm-1，α-螺旋的含量为40.45%；而当体积分数为2%时，1668 cm-1成为主峰（无规卷曲），α-螺旋和β-折叠含量显著下降（p<0.05），无规卷曲显著上升为31.58% （p<0.05）。结果表明白酒能够影响肌原纤维蛋白的结构和凝胶特性。

Raman spectroscopy was applied to study the structural changes caused by the volume fraction of distilled spirit on myofibrillar proteins extracted from Zhedong goose breast meat. The results indicated that increasing the volume fraction of the distilled spirit caused the solubility of myofibrillar protein to increase (p<0.05) and the surface hydrophobicity to decrease (p<0.05). As evidenced by scanning electron microscopy, a good gel property and a uniform microstructure were obtained when the volume fraction of the distilled spirit was low; however, with increasing volume fraction of the distilled spirit, the gel network pore size was increased and the water-holding capacity of proteins was decreased significantly (p<0.05). The increase in the volume fraction of distilled spirit caused conversions among the three conformations of the disulfide bond. For the control group, the main amide I Raman band was found at 1655 cm-1, with an α-helix of 40.45%. At a 2% volume fraction, the main band was found at 1668 cm-1 (random coil), the relative contents of the α-helix and β-sheet decreased significantly (p<0.05), and the random coil content increased significantly (34.40%) (p<0.05). This indicates that distilled spirit can affect the structure and gel properties of myofibrillar protein.

国家农业科技成果转化资金(2014GB2C220153)；宁波市科技局创新基金(2013C910017)；国家水禽产业体系基金（CARS-43-17）