波纹巴非蛤蛋白分离及其性质研究

Study on isolation and characterization of Paphia undulata protein

为了充分利用波纹巴非蛤蛋白质资源,对波纹巴非蛤蛋白质组成进行了分离,得到肌浆蛋白、肌原纤维蛋白、基质蛋白3种蛋白组分,并对其分子量分布和功能特性进行检测和分析。研究结果表明:肌浆蛋白组分占原料粗蛋白的31.2%,肌原纤维蛋白组分占45.42%,基质蛋白占20.69%,非蛋白氮占1.67%。SDS-PAGE电泳分析显示:肌浆蛋白组分亚基分子质量分布比较广泛,在200～29.0 kDa;肌原纤维蛋白组分分子质量大多介于66.4～200 kDa和29.0～38.0 kDa之间;基质蛋白组分在190 kDa、97 kDa、44 kDa、29 kDa附近有明显的条带。相同浓度下,温度升高肌浆蛋白和肌原纤维蛋白溶液浊度都上升,溶解度下降,变化趋势相似;pH对肌浆蛋白的浊度和溶解度影响不显著,在pH3.5～9.5,其溶解度均在71%以上,但肌原纤维蛋白浊度和溶解度受pH影响较大,当pH为4.5时,肌原纤维蛋白的溶解度降到最低,浊度达到最大;离子强度下降,肌原纤维蛋白溶液的浊度上升,溶解度下降。

Three types of Paphia undulata protein including myosinogen,myofibril protein and matrix protein were isolated and their molecular weight distribution and function characteristics were investigated in this paper to make full use of protein resources from Paphia undulata.Results indicated that the proportions of myosinogen,myofibril protein,matrix protein and nonprotein nitrogen（NPN） in Paphia undulata total protein were 31.2%,45.42%,20.69%,and 1.67%,respectively.Analysis results of SDS-PAGE electrophoresis showed that myosinogen strips distributed widely between 200 kDa and 29.0 kDa,and Myofibril protein strips mostly ranged from 66.4 to 200kDa and from 29.0 to 38.0kDa,and Matrix protein had obvious banding in 190kDa,97kDa,44kDa and 29kDa.Under the same protein concentration,the turbidity of myosinogen and myofibril protein rose,while the solubility reduced with the temperature increasing.Effects of pH on the solubility and turbidity of myosinogen were not obvious,and the solubility was above 71% under pH ranging from 3.5 to 9.5.However,effects of pH on the solubility and turbidity of myofibril protein were obvious.The solubility was lowest,while the turbidity was at its maximum at pH 4.5.Turbidity of myofibril protein rose,while solubility declined with ionic strength declining.