A novel method to depurate β-lactam antibiotic residues by administration of a broad-spectrum β-lactamase enzyme in fish tissues
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As a novel strategy to remove β-lactam antibiotic residues from fish tissues, utilization of β-lactamase, enzyme that normally degrades β-lactam structure-containing drugs, was explored. The enzyme (TEM-52) selectively degraded β-lactam antibiotics but was completely inactive against tetracycline-, quinolone-, macrolide-, or aminoglycosidestructured antibacterials. After simultaneous administration of the enzyme with cefazolin (a β-lactam antibiotic) to the carp, significantly lowered tissue cefazolin levels were observed. It was confirmed that the enzyme successfully reached the general circulation after intraperitoneal administration, as the carp serum obtained after enzyme injection could also degrade cefazolin ex vivo. These results suggest that antibiotics-degrading enzymes can be good candidates for antibiotic residue depuration.
Abstract
As a novel strategy to remove β-lactam antibiotic residues from fish tissues, utilization of β-lactamase, enzyme that normally degrades β-lactam structure-containing drugs, was explored. The enzyme (TEM-52) selectively degraded β-lactam antibiotics but was completely inactive against tetracycline-, quinolone-, macrolide-, or aminoglycosidestructured antibacterials. After simultaneous administration of the enzyme with cefazolin (a β-lactam antibiotic) to the carp, significantly lowered tissue cefazolin levels were observed. It was confirmed that the enzyme successfully reached the general circulation after intraperitoneal administration, as the carp serum obtained after enzyme injection could also degrade cefazolin ex vivo. These results suggest that antibiotics-degrading enzymes can be good candidates for antibiotic residue depuration.
참고문헌 (15)
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