Purification and Characterization of an Autolysin from Clostridium acetobutylicum.

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 Microbiol

authors

Webster JR,Reid SJ,Jones DT,Woods DR

doi

10.1128/AEM.41.2.371-374.1981

keywords:

subject

Has Abstract

pub_date

1981-02-01 00:00:00

pages

371-4

issue

2

eissn

0099-2240

issn

1098-5336

journal_volume

41

pub_type

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