Solubilization, Purification, and Properties of Membrane-BoundD -Glucono-δ-lactone Hydrolase fromGluconobacter oxydans
| Autor: | Yoshitaka Ano, Toshiharu Yakushi, Osao Adachi, Kazunobu Matsushita, Emiko Shinagawa |
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| Rok vydání: | 2009 |
| Předmět: |
Gluconobacter oxydans
Cations Divalent Gluconates Applied Microbiology and Biotechnology Biochemistry Acetobacteraceae Analytical Chemistry Divalent Lactones Bacterial Proteins Hydrolase Acetic acid bacteria Molecular Biology chemistry.chemical_classification Chromatography biology Organic Chemistry Membrane Proteins General Medicine Hydrogen-Ion Concentration biology.organism_classification Molecular Weight Enzyme Solubility chemistry Gluconolactonase Calcium Fermentation Carboxylic Ester Hydrolases Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 73:241-244 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.80554 |
| Popis: | Membrane-bound glucono-delta-lactonase (MGL) was purified to homogeneity from the membrane fraction of Gluconobacter oxydans IFO 3244. After solubilization with 1 M CaCl2, MGL was purified in the presence of Ca2+ and detergent. A single band corresponding to 60 kDa appeared in SDS-PAGE. The molecular weight of MGL was judged to be 120 k. Differently from cytoplasmic lactonases, MGL showed optimum pH in an acidic range of 5-5.5. It was highly sensitive to metal-chelating agents such as EDTA, and the lost MGL activity was restored to the original level by the addition of divalent cations such as Ca2+ or Mg2+. The purified MGL was strictly dependent on Ca2+ and underwent rapid denaturing precipitation on Ca2+ depletion even in the presence of detergent. This communication can be the first one dealing with the solubilization, purification and properties of MGL. |
| Databáze: | OpenAIRE |
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