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.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Webster JR,Reid SJ,Jones DT,Woods DRdoi
10.1128/AEM.41.2.371-374.1981keywords:
subject
Has Abstractpub_date
1981-02-01 00:00:00pages
371-4issue
2eissn
0099-2240issn
1098-5336journal_volume
41pub_type
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