SELECTIVE PRODUCTION OF EXTRACELLULAR PEROXIDASES FROM PHANEROCHAETE-CHRYSOSPORIUM IN AN AIRLIFT BIOREACTOR

Mn(II) concentrations had little effect on substrate uptake and growth rates, but they profoundly changed the composition of extracellular proteins. At low Mn(II) (0.3 ppm), Phanerochaete chrysosporium produced lignin peroxidase (LiP) isozymes (total activity=760 nmol ml-1 min-1), and the levels of Mn(II) peroxidase (MnP) isozymes were very low (130 nmol ml-1 min-1), whereas, with high Mn(II) (40 ppm), P. chrysosporium preferentially produced MnP isozymes (950 nmol ml-1 min-1), and LiPs were essentially absent. The airlift reactor provided a suitable low-shear environment for enzyme production by free mycelial pellets. This is a simple method to selectively produce LiP and MnP isozymes. © 1989.