Food Science and Technology Department
Department of Food Science and Technology: Faculty Publications
Document Type
Article
Date of this Version
1987
Abstract
Polyclonal antibodies to Escherichia coli β-galactosidase, β-glucuronidase, and glutamate decarboxylase were used in coagglutination tests for identification of these three enzymes in cell lysates. Enzyme capture assays were also developed for the detection of E. coli β-galactosidase and β-glucuronidase. The enzymes were released by using a gentle lysis procedure that did not interfere with antibody-enzyme interactions. All three enzymes were detected in 93% (51 of 55) of the E. coli strains tested by coagglutination; two of the three enzymes were identified in the remaining 7%. Of 42 non-E. coli tested by coagglutination, only four nonspecifically agglutinated either two or three of the anti-enzyme conjugates. Thirty-two (76%) non-E. coli isolates were negative by coagglutination for all three enzymes. The enzyme capture assay detected the presence of β-galactosidase in seven of eight and β-glucuronidase in all eight strains of E. coli tested. Some strains of β-galactosidase-positive Citrobacterfreundii and Enterobacter cloacae were also positive by the enzyme capture assay, indicating that the antibodies were not entirely specific for E. coli β-galactosidase; however, five other gas-positive non-E. coli isolates were negative by the enzyme capture assay. The coagglutination tests and enzyme capture assays were rapid and sensitive methods for the detection of E. coli ,β-galactosidase, β-glucuronidase, and glutamate decarboxylase.
Comments
Published in APPLIED AND ENVIRONMENTAL MICROBIOLOGY (1987) 53:5 p.1073-1077; Copyright 1987 American Society for Microbiology; Used by Permission