Characterization of an Extracellular Protease from the Insect Pathogen Xenorhabdus luminescens

AUTOR(ES)

Schmidt, Thomas M.

RESUMO

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.

Documentos Relacionados

• Bioluminescence of the insect pathogen Xenorhabdus luminescens.
• Purification and Characterization of an Extracellular Protease from Xenorhabdus nematophila Involved in Insect Immunosuppression
• Insecticidal Pilin Subunit from the Insect Pathogen Xenorhabdus nematophila
• Characterization of form variants of Xenorhabdus luminescens.
• Identification of an anthraquinone pigment and a hydroxystilbene antibiotic from Xenorhabdus luminescens.