Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens.
Xenorhabdus luminescens Hm cultured in gelatin broth produced a single extracellular protease. The protease was purified by a factor of 500 and characterized as a monomeric protein with an approximate molecular weight of 61,000. On the basis of inhibitor studies and its pH optimum, the protease was classified as an alkaline metalloprotease with a pH optimum near 8; the isoelectric point of the enzyme is 4.2 +/- 0.2. The protease may be a major factor in the ecology of X. luminescens, which is carried as a symbiom of some parasitic nematodes.
Schmidt
T M
TM
Center for Great Lakes Studies, University of Wisconsin-Milwaukee, 600 E. Greenfield Avenue, Milwaukee, Wisconsin 53204.
Bleakley
B
B
Nealson
K H
KH