AI Article Synopsis
- A fecal isolate from pigs, called Escherichia coli ECL12, produces an antimicrobial substance known as colicin ECL12, which effectively inhibits 20 strains of E. coli O157:H7 from both humans and cattle.
- The identification of the ECL12 strain involved various biochemical and morphological tests, and colicin ECL12 showed sensitivity to proteolytic enzymes.
- Purification of colicin ECL12 was accomplished through cell extraction and ion-exchange chromatography, revealing a single protein with an approximate molecular weight of 65,000 during analysis.
Article Abstract
A swine fecal isolate, identified as Escherichia coli ECL12, was found to produce an antimicrobial substance designated as colicin ECL12. Colicin ECL12 was inhibitory against 20 strains of E. coli O157:H7 previously isolated from both human and bovine feces. Identification of the producer strain was determined phenotypically by biochemical and morphological tests. Colicin ECL12 was sensitive to several proteolytic enzymes. Adsorption of colicin ECL12 to sensitive cells of E. coli O157:H7 was bactericidal, resulting in a 2 log reduction in viable cell counts. Colicin ECL12 was purified from strain ECL12 by cell extraction and ion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of colicin ECL12 resolved a single protein with a molecular weight of approximately 65,000.
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| http://dx.doi.org/10.4315/0362-028X-60.12.1520 | DOI Listing |
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Isolation and Purification of Colicin ECL 12, a Bacteriocin That Inhibits Strains of Escherichia coli O157:H7 .
J Food Prot
December 1997
Department of Animal Science, Iowa State University, Ames, Iowa 50011, USA.
Article Synopsis
- A fecal isolate from pigs, called Escherichia coli ECL12, produces an antimicrobial substance known as colicin ECL12, which effectively inhibits 20 strains of E. coli O157:H7 from both humans and cattle.
- The identification of the ECL12 strain involved various biochemical and morphological tests, and colicin ECL12 showed sensitivity to proteolytic enzymes.
- Purification of colicin ECL12 was accomplished through cell extraction and ion-exchange chromatography, revealing a single protein with an approximate molecular weight of 65,000 during analysis.
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