Purification and properties of aldehyde dehydrogenase from Aspergillus nidulans |
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| Institution: | 1. Departamento de Microbiología e Inmunología, Facultad de Ciencias Exactas, Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Ruta Nacional 36, Km 601, 5800 Río Cuarto, Córdoba, Argentina;2. Institute of Sciences of Food Production, CNR, Via Améndola 122/0, 70126 Bari, Italy;1. Microbial Safety Team, National Institute of Agricultural Science, Rural Development Administration, Wanju 55365, Republic of Korea;2. Department of Medical Biotechnology, Soonchunhyang University, Asan 31538, Republic of Korea;1. Department of Agricultural, Food and Environmental Sciences, University of Perugia, Borgo XX Giugno 74, 06121 Perugia, Italy;2. Centre for Analytical Chemistry, Department of Agrobiotechnology (IFA-Tulln), University of Natural Resources and Life Sciences (BOKU), Vienna, Konrad Lorenz Strasse 20, A-3430 Tulln, Austria |
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| Abstract: | - 1.1. Aspergillus nidulans produces aldehyde dehydrogenase (ALD-DH) only when grown in the presence of ethanol, threonine or acetoacetic acid as inducer. Enzyme formation is inhibited by glucose in the growth medium.
- 2.2. ALD-DH is purified by a rapid procedure using Cibacron Blue Affinity Chromatography with specific inhibitoe elution by NAD plus 2:2′ dithiodipyridine or 2:4 disulfiram.
- 3.3. The pure native enzyme has a Mr=265,000 and a subunit Mr of 540,000. Its optimum pH is 8.5; its preferred substrate is acetaldehyde and it can use either NAD or NADP.
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