This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Webster, J. R. Articles by Woods, D. R. Search for Related Content PubMed PubMed Citation Articles by Webster, J. R. Articles by Woods, D. R. Agricola Articles by Webster, J. R. Articles by Woods, D. R.

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1981 February; 41(2): 371-374

Purification and Characterization of an Autolysin from Clostridium acetobutylicum

Department of Microbiology, University of Cape Town, Rondebosch 7700, South Africa

ABSTRACT

A proteinaceous substance with antibiotic-like activity, resembling that of a bacteriocin, was isolated from an industrial-scale acetone-butanol fermentation of Clostridium acetobutylicum. The substance, purified by acetone precipitation, diethylaminoethyl cellulose chromatography, and polyacrylamide gel electrophoresis, was characterized as a glycoprotein with a molecular weight of 28,000. The glycoprotein was partially inactivated by certain protease enzymes. It had no effect on deoxyribonucleic acid, ribonucleic acid, or protein synthesis, and it did not result in the loss of intracellular adenosine triphosphate. The glycoprotein lysed sodium dodecyl sulfate-treated cells and cell wall preparations, and therefore it is referred to as an autolysin. The autolysin gene appeared to be chromosomal since plasmid deoxyribonucleic acid was not detected in the C. acetobutylicum strain.