Effect of simultaneous beta-lactamase inhibitor protein expression on cellular beta-lactamase activity

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dc.contributorGraduate Program in Chemical Engineering.
dc.contributor.advisorÖzkırımlı, Elif.
dc.contributor.advisorSarıyar, Berna.
dc.contributor.authorYalaz, Kadriye Simay.
dc.date.accessioned2023-03-16T11:06:27Z
dc.date.available2023-03-16T11:06:27Z
dc.date.issued2012.
dc.description.abstractβ-lactam antibiotics are commonly used in the treatment of bacterial infections. However, due to underuse and misuse of β-lactam antibiotics, bacteria have developed mechanisms that counteract β-lactam antibiotics. The most common mechanism is production of TEM-1 β-1actamase that hydrolyzes the β-lactam ring and enables bacteria to gain antibiotic resistantance. β-lactamase-inhibitory protein (BLIP), a 165 amino acid protein produced by Streptomyces clavuligerus, is a high affinity β-lactamase inhibitor. In this study, the inhibitory effect of BLIP was investigated by examining growth profiles, cell viability and in-vivo β-lactamase activity of recombinant cells simultaneously expressing β-lactamase and BLIP. β-lactamase activity per viable cell was determined in the absence and presence of BLIP. The presence of both BLIP and β-lactamase was verified by SDS-PAGE and Native-PAGE analysis. In the absence of BLIP, E. coli BL21(DE3) (pUC18 + pET-26EA) and E. coli BL21(DE3) (pUC18 + pET-26b(+)) cells showed comparable -lactamase activity. The activity of β-lactamase in the periplasmic extract of E. coli BL21(DE3) (pUC18 + pET-26EA) cells decreased considerably when R-TEM-1 β-lactamase and BLIP were expressed simultaneously.
dc.format.extent30 cm.
dc.format.pagesxvi, 65 leaves ;
dc.identifier.otherCHE 2012 Y36
dc.identifier.urihttps://digitalarchive.library.bogazici.edu.tr/handle/123456789/14612
dc.publisherThesis (M.S.) - Bogazici University. Institute for Graduate Studies in Science and Engineering, 2012.
dc.relationIncludes appendices.
dc.relationIncludes appendices.
dc.subject.lcshBeta lactam antibiotics.
dc.titleEffect of simultaneous beta-lactamase inhibitor protein expression on cellular beta-lactamase activity

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