Purification and some properties of an esterase from yeast |
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| Affiliation: | 1. Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, Einsteinweg 55, 2300 RA Leiden, The Netherlands;2. Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands;1. Institute of Biochemistry and Biology, General Botany, University of Potsdam, Maulbeerallee 3, 14469 Potsdam, Germany;2. Department of Biodiversity and Landscape Ecology, Faculty of Biology and Chemistry, Osnabrück University, Barbarastraße 13, 49076 Osnabrück, Germany;3. Institute of Biodiversity and Landscape Ecology (IBL), Hafenweg 31, 48155 Münster, Germany;1. Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands;2. Departamento de Micologia Prof. Chaves Batista, Universidade Federal de Pernambuco, Av. Prof. Moraes Rego, s/n, Centro de Biociências, Cidade Universitária, CEP: 50670-901 Recife, PE, Brazil;3. Swedish University of Agricultural Sciences, Department of Molecular Sciences, Box 7015, SE-750 07 Uppsala, Sweden;4. National Genomics Infrastructure-Sweden, Science for Life Laboratory, Department of Immunology, Genetics and Pathology, Uppsala University, BMC, Box 815, SE-752 37 Uppsala, Sweden;5. Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100193, PR China;6. Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kongens Lyngby, Denmark |
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| Abstract: | ![]()
An esterase was isolated and purified from baker's yeast by ammonium sulfate precipitation and column chromatographies on Sephacryl S-200, DEAE-Sephacel, chromatofocusing, and DEAE-Sephacel again. The molecular weight of the enzyme was approximately 84,000 on Sephadex G-100 and 40,000 by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis, suggesting a dimer for the activity. This enzyme hydrolyzed short-chain naphthyl esters and p-nitrophenyl esters, and its activity was strongly inhibited by mercuric compounds. The esterase appeared to be an arylesterase (EC 3.1.1.2) and its optimum pH was 8.0 at 30°C. |
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