Purification and characterization of a cephalosporin esterase from Rhodosporidium toruloides
| العنوان: | Purification and characterization of a cephalosporin esterase from Rhodosporidium toruloides |
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| المؤلفون: | Michael Politino, Sean M. Tonzi, John J. Usher, William V. Burnett, Guna Romancik |
| المصدر: | Applied and Environmental Microbiology. 63:4807-4811 |
| بيانات النشر: | American Society for Microbiology, 1997. |
| سنة النشر: | 1997 |
| مصطلحات موضوعية: | medicine.drug_class, Molecular Sequence Data, Cephalosporin, Rhodosporidium toruloides, Applied Microbiology and Biotechnology, Esterase, chemistry.chemical_compound, Enzyme Stability, medicine, Amino Acid Sequence, Isoelectric Point, chemistry.chemical_classification, Binding Sites, Ecology, biology, Molecular mass, Cephalosporin-C deacetylase, Basidiomycota, Temperature, Cephalosporin C, biology.organism_classification, Molecular Weight, Kinetics, Enzyme, Isoelectric point, chemistry, Biochemistry, Carboxylic Ester Hydrolases, Bacillus subtilis, Research Article, Food Science, Biotechnology |
| الوصف: | A novel cephalosporin esterase (EC 3.1.1.41) from Rhodosporidium toruloides was purified to gel electrophoretic homogeneity. The enzyme is a glycoprotein with a molecular mass of 80 kDa. Upon deglycosylation, several forms of the enzyme were observed with a molecular mass range between 60 and 66 kDa. The isoelectric point of the enzyme is approximately 5.6, with the pH optimum for activity occurring at 6.0. The optimal activity of the enzyme occurred at 25 degrees C, with the enzyme rapidly losing activity at temperatures above 25 degrees C. The enzyme deacetylated a variety of cephalosporin derivatives, including cephalosporin C; the Km for this substrate is 51.8 mM, and the Vmax is 7.9 mumol/min/mg. In addition to cephalosporins, the enzyme hydrolyzed short-chain p-nitrophenyl esters, with the activity decreasing with increasing ester chain length. The enzyme also has the ability to acetylate desacetyl cephalosporins in high yields under mild conditions in the presence of various acetyl donors. A comparison of the physical properties of the esterase with those of other well-characterized cephalosporin esterases indicates that the enzyme is unique in this class. |
| تدمد: | 1098-5336 0099-2240 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a7513c4725cc82cd82125019f9ceed5 https://doi.org/10.1128/aem.63.12.4807-4811.1997 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....2a7513c4725cc82cd82125019f9ceed5 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10985336 00992240 |
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