APPLICATION OF THE PCLODF13 BACTERIOCIN RELEASE PROTEIN IN THE RELEASE OF HETEROLOGOUS PROTEINS BY ESCHERICHIA-COLI - PRODUCTION OF PLANT ALPHA-GALACTOSIDASE
F. Vanderwal et al., APPLICATION OF THE PCLODF13 BACTERIOCIN RELEASE PROTEIN IN THE RELEASE OF HETEROLOGOUS PROTEINS BY ESCHERICHIA-COLI - PRODUCTION OF PLANT ALPHA-GALACTOSIDASE, Biotechnology letters, 17(8), 1995, pp. 815-820
The bacteriocin release protein (BRP) mediated release of several euka
ryotic proteins was studied in Escherichia coil. The genes for the pla
nt proteins a-galactosidase and thaumatin, and for the mammalian prote
ins prochymosine and prophospholipase A(2), were cloned behind the Omp
A signal peptide. The alpha-galactosidase was expressed and secreted i
nto the periplasm. Prochymosine and thaumatin were poorly expressed. R
elease experiments showed that about 5 mg/l of alpha-galactosidase was
excreted into the extracellular medium upon induction of the BRP.