Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated peptidoglycan

Article Abstract:

An extracellular enzyme capable oflyzing non-N-acetylated peptidoglycan has been recovered and purified from Clostridium acetobutylicum ATCC 824 cells. This enzyme has been characterized as a muramidase with a molecular weight of 41,000 and an acidic isoelectric point of 3.8. It is the first muramidase that cleaves only non-N-acetylated peptidoglycans. Its enzymatic activity is inhibited by N-acetylglucosamine and glucosamine and enhanced by choline and ethanolamine.

Lysozyme

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Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities

Article Abstract:

The Strep tag II-Fe-only hydrogenase of Clostridium acetobutylicum is purified. An electron paramagnetic resonance (EPR) analysis of the thionin-oxidized HydA(sub Ca) protein indicates a characteristic rhombic EPR signal that is typical for the oxidized H cluster of Fe-only hydrogenases.

Germany, Analysis, Electron paramagnetic resonance

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Development of a sensitive gene expression reporter system and an inducible promoter-repressor system for Clostridium acetobutylicum

Article Abstract:

Research has been conducted on Clostridium acetobutylicum ATCC 824. The authors describe the development of the sensitive gene expression system for this strain carried out via the use of a customized expression cassette.

France, Physiological aspects, Environmental aspects, Genetic aspects, Microbiology, Gene expression, Microbial populations, Microbial ecology

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