研究了类人胶原蛋白Ⅱ在基因工程菌E.coli BL213.7中的表达与纯化。经高密度发酵及代谢调控,重组菌在12.8L发酵罐中的最终菌体密度约为150。菌体经高压匀浆破碎、沉淀、超滤、阳离子交换色谱纯化后,表达产物纯度达96.4%,总回收率71.6%。
The expression and purification of recombinant human-like collagen Ⅱ in E. coli BL21 3.7 was studied. By high cell density fermentation and metabolic regulation and control, the cell density reached around 150 in 12.8L fermentor. The purified human-like collagen Ⅱ was abtained through the following procedures: high pressure homogenization, sedimentation, ultrafiltration and cation exchange chromatography. The purity of product was 96.4 % with the overall recovery of 71.6%.