摘要 以小米分离蛋白为研究对象,通过转谷氨酰胺酶交联酶改性后,对其不同条件下的溶解性进行分析研究,通过SDS-PAGE电泳对小米酶改性蛋白组分进行亚基分析。结果表明,在不同处理情况下,小米酶改性蛋白在pH 5处溶解度最小,故等电点应在pH 5附近;随盐离子浓度升高,蛋白溶解度呈现先下降后上升再下降现象;温度升高,蛋白溶解度呈现先上升后趋于稳定现象;SDS-PAGE试验结果显示,小米酶改性蛋白亚基大部分分子质量大于66.2k Da,含二硫键的亚基占大部分,在不同pH下,等电点附近沉淀的亚基数量最多,进一步印证等电点附近蛋白的溶解度的变化规律;在不同离子强度下的溶解度差异,只是整体亚基的溶解度差异,并无亚基溶解度的特异差别,在不同温度下,最接近分子质量14.4 kDa的亚基不易聚集形成不溶性聚集体。 The millet protein isolate taken as the research object,its solubility under different conditions was analyzed after transglutaminase crosslinking enzyme was modified,and subunit analysis of millet enzyme modified protein components was conducted by SDS-PAGE.The results showed that under different treatments,the solubility of millet enzyme modified protein was the smallest at pH 5,so the isoelectric point should be near pH 5.With the increase of salt ion concentration,the solubility of protein decreased firstly,then increased and then decreased.As the temperature rose,the solubility of the protein increased and then stabilized.The SDS-PAGE results showed that the molecular weight of most of the mi-modified protein subunits was greater than 66.2 kDa,and the subunits containing disulfide bonds accounted for the majority.Under different pH,the number of subunits precipitated near the isoelectric points was the largest,which further confirmed the change rule of the solubility of proteins near the isoelectric points.The solubility difference under different ion intensities was only the solubility difference of the whole subunit,but there was no specific difference in the solubility of the subunit.At different temperatures,the subunit closest to the molecular weight of 14.4 kDa was not easy to aggregate into insoluble aggregates.
机构地区 山西农业大学食品科学与工程学院 山西农业大学校医院
出处 《食品工业》 CAS 北大核心 2021年第2期111-115,共5页 The Food Industry
基金 山西省重点研发计划重点项目“山西功能农业共性关键技术研究与示范(201703D211001-06) 山西农业大学博士科研启动(2016ZZ06)。
关键词 小米蛋白 TG酶 酶交联技术 分离提取 SDS-PAGE 亚基 millet protein TG enzyme enzyme cross-linking technique separate extraction SDS-PAGE subunit
分类号 TS2 [轻工技术与工程—食品科学与工程]
