Crévieu I, Bérot S, Guéguen J
INRA, Laboratoire de biochimie et technologie des protéines, Nantes, France.
Nahrung. 1996 Oct;40(5):237-44. doi: 10.1002/food.19960400502.
The buffer extractable proteins of pea, albumins and globulins, were successively extracted in a large amount at a pilot scale. In order to preserve as much as possible the native structure of proteins, a selective solubilization step procedure was performed. Firstly, albumins were extracted with acetate buffer and secondly globulins with phosphate buffer of high ionic strength. Each extract was desalted by diafiltration without protein precipitation. From 15 kg of flour, 380 g of albumin fraction and 1000 g of globulin fraction were obtained with a protein content of 86.0% and 90.7% of dry matter respectively. The characterisation of albumin and globulin fractions by electrophoresis, ultracentrifugation and anion-exchange chromatography, showed that the cross-contamination of these two fractions was minimal.
豌豆中的缓冲液可提取蛋白，即清蛋白和球蛋白，在中试规模下被大量连续提取。为尽可能保留蛋白质的天然结构，进行了选择性增溶步骤。首先，用乙酸盐缓冲液提取清蛋白，其次用高离子强度的磷酸盐缓冲液提取球蛋白。每种提取物通过渗滤脱盐，且无蛋白质沉淀。从15千克面粉中，分别获得了380克清蛋白组分和1000克球蛋白组分，其蛋白质含量分别为干物质的86.0%和90.7%。通过电泳、超速离心和阴离子交换色谱对清蛋白和球蛋白组分进行表征，结果表明这两个组分的交叉污染极小。
