籽瓜种子蛋白对肌原纤维蛋白功能的影响

The Effect of Watermelon Seed Protein on the Function of Myofibrillar

本研究以籽瓜种子为原料,利用碱溶酸沉方法提取籽瓜种子蛋白,在40、60、80℃条件下获得不同籽瓜种子蛋白,分别进行分子质量、溶解度测定,并与肌原纤维蛋白形成凝胶,对凝胶作用力、弹性、回弹性、粘结性、水相分度、白度进行试验。结果表明,40~80℃范围内随着提取温度的升高,籽瓜种子蛋白溶解度先升高后降低差异显著(P<0.05),并获得4个吸收峰,峰1为699~103ku的大分子蛋白聚集体,峰2、峰3分别为340、212 ku的球蛋白,及10~54 ku部分清蛋白、球蛋白的亚基,随着碱溶温度继续升高,峰2、峰3逐渐消失。籽瓜种子蛋白与肌原纤维蛋白形成凝胶的三维网状结构稳定性通过疏水键、氢键、以及二硫键维持,其中疏水键、氢键为主要作用力。碱溶温度为60℃时,WPS与MP形成凝胶弹性较好、保水性较好,差异显著(P<0.05)。随着温度的增加,凝胶白度逐渐加,WPS结构发生改变、变性,差异显著(P<0.05)。由此可知,温度对籽瓜种子蛋白结构、功能影响较大,不同碱溶温度提取的籽瓜种子蛋白对肌原纤维蛋白功能影响差异显著,碱溶温度为60℃时,获得籽瓜种子蛋白与肌原纤维蛋白形成的凝胶有利于改善对肉制品品质,可作为非肉蛋白稳定剂添加到猪肉制品中。

The watermelon seed -solution and acid- isolation method was selected . Under the could be gained. The molecular weight, solubility as the raw material to extract the watermelon seed protein by alkali temperature of 40,60 and 80 ℃, different watermelon seed protein test was conducted and fibrillin formed gelate. Experiments were conducted on gel acting force, elasticity, rebound resilience, caking property, aqueous phase degree and whiteness. The studies showed that solubility of the WPS increases with the following decrease as the increasing temperature. There were four absorption peaks as follows. The Mw of peak 1 was 699 - 103 ku as the macromolecule protein aggregation. The Mw of peak 2 and peak 3 were 340 and 212 ku, respectively, as the different sedimentation coefficient of globulin. The Mw of peak 4 was 10 - 54 ku as the subunit of some albumin and globulin. The peak 2 and 3 disappeared gradually as the increasing temperature. The stability of the three - dimensional network structure was held by the disulfide bond, and especially the hydrophobic bond, hydrogen bond. The WPS and MP form a gel as the alkali liquor temperature 60 ℃, of which elasticity and water distribution was suitable for the application of pork products. The temperature of alkali liquor was important for the protein denaturation. Taken together, the WPS could be added to the pork products as the non meat proteins stabilizer.