Penicillin Acylase Production By Micrococcus luteus and Staphylococcus spp. Isolated from Soda Lake.
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چکیده
منابع مشابه
Biochemical properties of penicillin amidohydrolase from Micrococcus luteus.
Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C. The penicillin amidohydrolase was deactivated rapi...
متن کاملDegradation of Pyridine by Micrococcus luteus Isolated from Soil.
An organism capable of growth on pyridine was isolated from soil by enrichment culture techniques and identified as Micrococcus luteus. The organism oxidized pyridine for energy and released N contained in the pyridine ring as ammonium. The organism could not grow on mono- or disubstituted pyridinecarboxylic acids or hydroxy-, chloro-, amino-, or methylpyridines. Cell extracts of M. luteus coul...
متن کاملProduction of Penicillin Acylase.
The production of penicillin acylase by Escherichia coli Ny.I/3-67 has been increased by phenylacetic acid and phenoxyacetic acid, which themselves strongly inhibit the function of this specific enzyme. Other carbonic acids also increased penicillin acylase production, but to a lesser degree; they also weakly inhibited enzyme function. The production of this enzyme was effectively repressed wit...
متن کاملStaphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins.
Major peptidoglycan transglycosylase activities, which synthesize uncross-linked peptidoglycan from lipid-linked precursors, were solubilized from the membranes of Staphylococcus aureus and Micrococcus luteus and were partially purified. The transglycosylase activities were separated from penicillin-binding proteins by solubilization and by purification steps. Therefore, we concluded that these...
متن کاملMolecular properties of succinate dehydrogenase isolated from Micrococcus luteus (lysodeikticus).
Succinate dehydrogenase (EC 1.3.99.1) of Micrococcus luteus was selectively precipitated from Triton X-100-solubilized membranes by using specific antiserum. The precipitated enzyme contained equimolar amounts of four polypeptides with apparent molecular weights of 72,000, 30,000, 17,000, and 15,000. The 72,000 polypeptide possessed a covalently bound flavin prosthetic group and appeared to be ...
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ژورنال
عنوان ژورنال: IOSR Journal of Pharmacy (IOSRPHR)
سال: 2012
ISSN: 2319-4219,2250-3013
DOI: 10.9790/3013-0220296301