Deng Yejun, Huang Lixin, Zhang Caihong, Xie Pujun
Institute of Chemical Industry of Forest Products, CAF; National Engineering Lab. for Biomass Chemical Utilization, Key and Open Lab. of Forest Chemical Engineering, SFA, Key Lab. of Biomass Energy and Material, Number 16 Suojin wucun, Xuanwu District, Nanjing, 210042 Jiangsu Province People's Republic of China.
2Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Nanjing Forestry University, Nanjing, 210037 People's Republic of China.
J Food Sci Technol. 2020 Feb;57(2):764-774. doi: 10.1007/s13197-019-04109-6. Epub 2019 Sep 16.
Chinese quince seed proteins were sequentially extracted based on the modified Osborne method. Investigations showed that albumin and glutelin were the major fractions. The physicochemical and functional properties of these two fractions were determined. The results showed that both albumin and glutelin posed appropriate essential amino acid composition and met the minimum recommendation (World Health Organization/Food and Agriculture Organization) for adult diet, except for methionine. The hydrophobicity of albumin and glutelin were 1063.56 and 1170.21, respectively. According to differential scanning calorimeter analysis, the denaturation temperature of albumin and glutelin was 101.44 °C and 108.36 °C respectively, and the glutelin fraction had a better thermal stability. The solubility and apparent viscosity of albumin and glutelin were presented to be greatly influenced by pH values. The water holding capacity and oil adsorption capacity of glutelin were 5.44 g/g and 8.15 g/g, higher than those of albumin which were 3.76 g/g and 3.71 g/g, respectively. Circular dichroism determination revealed albumin and glutelin were mainly composed by α-helix and random coil structures. Albumin and glutelin presented the potential as favorable nutrition and functional additive in food industries.
基于改良的奥斯本方法对榅桲种子蛋白进行了顺序提取。研究表明，清蛋白和谷蛋白是主要组分。测定了这两个组分的理化性质和功能特性。结果表明，除蛋氨酸外，清蛋白和谷蛋白均具有合适的必需氨基酸组成，满足成人饮食的最低推荐量（世界卫生组织/联合国粮食及农业组织）。清蛋白和谷蛋白的疏水性分别为1063.56和1170.21。根据差示扫描量热分析，清蛋白和谷蛋白的变性温度分别为101.44℃和108.36℃，谷蛋白组分具有更好的热稳定性。清蛋白和谷蛋白的溶解度和表观粘度受pH值影响较大。谷蛋白的持水能力和吸油能力分别为5.44 g/g和8.15 g/g，高于清蛋白的3.76 g/g和3.71 g/g。圆二色性测定表明，清蛋白和谷蛋白主要由α-螺旋和无规卷曲结构组成。清蛋白和谷蛋白在食品工业中具有作为良好营养和功能添加剂的潜力。
