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. 1988 Nov;54(11):2793-7.
doi: 10.1128/aem.54.11.2793-2797.1988.

Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens

T M Schmidt  1 , B Bleakley, K H Nealson
Affiliations

Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens

T M Schmidt et al. Appl Environ Microbiol. 1988 Nov.

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.

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