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作 者:贾润红[1] JIA Run-hong(Elementary Education College,Lianyungang Normal College,Lianyungang 222006,Jiangsu,China)
机构地区:[1]连云港师范高等专科学校初等教育学院,江苏连云港222006
出 处:《粮食与油脂》2021年第3期107-110,共4页Cereals & Oils
基 金:2019年江苏省青蓝工程中青年学术带头人培养对象;2021年连云港市第六期“521工程”第三层次培养对象;2020年度连云港师范高等专科学校高级别培育项目。
摘 要:利用花生蛋白和葡聚糖进行糖基化反应,研究不同pH(3.0~8.0)对糖基化花生蛋白乳化特性的影响,并测定了糖基化花生蛋白的Zeta电位、粒径、表面疏水性、游离氨基酸的含量、游离巯基的含量以及乳化性。结果表明:pH接近蛋白质等电点时,蛋白质之间可发生聚集,具有特大粒径、较低Zeta电位和较低的表面电荷,导致乳化性降低。pH偏离蛋白质等电点时,蛋白质结构可展开,有利于快速吸附到油水界面,具有更多的表面电荷和更小的粒径,游离巯基的数量逐渐减少,并提高了乳化性。此外,蛋白质在酸性环境中的表面疏水性要高于碱性环境,而游离氨基酸含量要低于碱性环境。Peanut protein and dextran were used for glycosylation,and the effect of different pH values(3.0~8.0)on the emulsification characteristics of glycosylated peanut protein was studied.Zeta potential,particle size,surface hydrophobicity,free amino acid content,free sulfhydryl content and emulsifying property of glycosylated peanut protein were determined.The results showed that when the pH was close to the isoelectric point of proteins,the aggregation between proteins could occur,with large particle size,low zeta potential and low surface charge,resulting in the reduction of emulsification.When pH deviated from the isoelectric point of protein,the protein structure could be expanded,which was conducive to the rapid adsorption to the oil-water interface.With more surface charges and smaller particle size,the number of free sulfhydryl groups gradually decreased,and the emulsifying property was improved.In addition,the surface hydrophobicity of protein in acidic environment was higher than that in alkaline environment,while the content of free amino acids was lower than that in alkaline environment.
分 类 号:TS201.21[轻工技术与工程—食品科学]
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