HETEROLOGOUS PROTEIN-PRODUCTION IN ACREMONIUM-CHRYSOGENUM - EXPRESSION OF BACTERIAL CEPHALOSPORIN-C ACYLASE AND HUMAN THROMBOMODULIN GENES

We have developed an efficient expression system for foreign genes in Acremonium chrysogenum. After inserting the foreign gene between the p hosphoglycerate kinase (PGK) promoter and a terminator derived from A, chrysogenum, multiple copies of this expression unit are tandemly lig ated into cosmids and the resultant cosmids are introduced into A, chr ysogenum. We expressed Pseudomonas cephalosporin C acylase and a human thrombomodulin mutant protein containing the fourth, fifth, and sixth epidermal growth factor (EGF)-like structures (E456), The acylase act ivity in the transformants obtained using our system was several times higher than that in the transformants without the use of the system, The acylase proteins expressed had enzymatic and immunochemical proper ties identical to those of authentic acylase, The transformants with t he expression plasmid for E456 secreted biologically active E456 prote in into the culture medium, The amino terminal sequence of the purifie d E456 was identical to that of recombinant E456 obtained using mammal ian cells.