摘要
以牛背最长肌为原料,研究豌豆蛋白对其盐溶蛋白十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate and polyacrylamide gelelectrophoresis, SDS-PAGE)、溶解度、表面疏水性、巯基、二硫键含量、乳化性等理化性质及二级结构的影响,并探讨了豌豆蛋白与盐溶蛋白凝胶形成过程中化学作用力类型。结果表明,SDS-PAGE电泳中,豌豆蛋白中的vicilin(7S)、legA和legB分别与盐溶蛋白中的肌动蛋白、肌钙蛋白T和肌钙蛋白C结合。当豌豆蛋白添加质量浓度为0.08 g/mL时,盐溶蛋白的表面疏水性上升明显(P<0.05);二硫键含量在豌豆蛋白添加浓度超过0.12 g/mL后,迅速上升(P<0.05)。随豌豆蛋白添加浓度的增加,盐溶蛋白总巯基和表面活性巯基含量下降,浊度和乳化性上升;溶解度呈先升高后下降趋势,在添加浓度为0.04 g/mL时最大。豌豆蛋白添加质量浓度与α-螺旋、表面活性巯基含量等均呈显著负相关,与β-折叠、β-转角、无规则卷曲、二硫键含量、表面疏水性等呈显著正相关;疏水相互作用是豌豆蛋白-牛肉盐溶蛋白凝胶网络结构形成中最主要化学作用力。
Salt-soluble proteins were extracted from bovine longissimus thoracis muscles(BLTM). Effects of pea protein on physicochemical properties(SDS-PAGE, solubility, surface hydrophobicity, sulfhydryl group, disulfide bond content, emulsifying properties) and secondary structures of salt-soluble proteins from BLTM were studied. Additionally, the types of chemical bonds formed during the gelling of pea protein and salt-soluble proteins were explored. The SDS-PAGE results indicated that vicilin(7 S), legA, and legB in pea protein were bound to actin, troponin T, and troponin C in salt-soluble proteins. When 0.08 g/mL pea protein was added, the surface hydrophobicity of salt-soluble protein increased significantly(P<0.05). Moreover, the disulfide bond content increased rapidly when more than 0.12 g/mL pea protein was added(P<0.05). As the concentration of pea protein increasing, the contents of both total sulfhydryl and surface active sulfhydryl of salt-soluble proteins decreased, while their turbidity and emulsibility increased. Furthermore, the solubility of salt-soluble proteins increased first and then decreased, with the maximal reached when 0.04 g/mL pea protein was added. Additionally, the amount of pea protein added was negatively correlated with α-helix and surface active sulfhydryl content, and it was positively correlated with β-folding, β-rotation, irregular curl, disulfide bond content, and surface hydrophobicity of salt soluble proteins. Besides, hydrophobic interaction was the most important chemical force when forming pea protein-BLTM salt soluble proteins gel network structure.
引文
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