Ward P P, Piddington C S, Cunningham G A, Zhou X, Wyatt R D, Conneely O M
Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Biotechnology (N Y). 1995 May;13(5):498-503. doi: 10.1038/nbt0595-498.
We previously reported the production of limited quantities of biologically active recombinant human lactoferrin in the filamentous fungus Aspergillus oryzae. In the present study, we report a modification of this production system combined with a classical strain improvement program that has enabled production of levels of recombinant human lactoferrin in excess of 2 g/l. The protein was expressed in Aspergillus awamori as a glucoamylase fusion polypeptide which was secreted into the growth medium and processed to mature human lactoferrin by an endogenous KEX-2 peptidase. The recombinant protein retains full biological activity in terms of its ability to bind iron and human enterocyte receptors. Furthermore, the recombinant protein functions as a potent broad spectrum antimicrobial protein.
我们之前报道过在丝状真菌米曲霉中生产少量具有生物活性的重组人乳铁蛋白。在本研究中，我们报告了对该生产系统的改进，并结合经典的菌株改良程序，使得重组人乳铁蛋白的产量超过了2 g/l。该蛋白在泡盛曲霉中作为一种糖化酶融合多肽表达，分泌到生长培养基中，并被内源性KEX-2肽酶加工成成熟的人乳铁蛋白。就其结合铁和人肠细胞受体的能力而言，重组蛋白保留了完整的生物活性。此外，重组蛋白还具有强效的广谱抗菌蛋白功能。
