Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein.

Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Research Abstract Details 

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Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Abstract Text:

The applicability of a beta-lactam receptor protein for detection of beta-lactam antibiotics in milk using surface plasmon resonance (SPR) biosensor technology was investigated. The advantage of using a receptor protein instead of antibodies for detection of beta-lactams is that a generic assay, specific for the active form of the beta-lactam structure, is obtained. Two assays based on the enzymatic activity of the DD-carboxypeptidase from Actinomadura R39 were developed, using a Biacore SPR biosensor. The carboxypeptidase converts a tri-peptide into a di-peptide, a reaction which is inhibited in the presence of beta-lactams. Polyclonal antibodies against the 2 peptides were developed and used to measure the amount of enzymatic product formed (di-peptide assay) or the amount of remaining enzymatic substrate (tri-peptide assay), respectively. The 2 assays showed similar performances with respect to detection limits (1.2 and 1.5 microg/kg, respectively) and precision (coefficient of variation <5%) for penicillin G in milk. Several other beta-lactams were detected at or near their respective maximum residue limit. Furthermore, the 2 peptide assays were evaluated against 5 commercial kit tests in the screening of 195 producer milk samples. The biosensor assays showed 0% false-negative and 27% false-positive results, whereas the figures were 0% false-negative and 27-53% false-positive results for other screening tests investigated.

Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Publishing Authors By Initials

For similar organic chemicals: amides: lactams: beta-lactams research abstracts see: organic chemicals: amides: lactams: beta-lactams research

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Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Journal Published:

PUBLICATION TYPE: Review

Journal: Journal of AOAC International

VOLUME: 89

Page Numbers: 832-7

Journal Abbreviation: J AOAC Int

ISSN: 1060-3271

DAY: 17

MONTH: 03

YEAR: 2008

Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Information

Number of References: 22

LANGUAGE: eng

NlmUniqueID: 9215446

Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Keywords Mesh Terms:

KEYWORDS: beta-Lactams

MESH TERMS: analysis

Chemical & Substance for Abstract: Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein. Information

Substance Name: Carboxypeptidases

Registry Number: EC 3.4.-

Grant and Affiliation Information for Biosensor analysis of beta-lactams in milk using the carboxypeptidase activity of a bacterial penicillin binding protein.

AFFILIATION: Swedish University of Agricultural Sciences, Department of Food Science, PO Box 7051, 750 07 Uppsala, Sweden. ase.sternesjo@lmv.slu.se

Country: United States

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MEDLINETA: J AOAC Int

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