Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens

Abstract

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.