Purification and characterization of intracellular galactose oxidase from Dactylium dendroides |
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| Authors: | M H Mendon?a G T Zancan |
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| Affiliation: | 1. School of Life Sciences, Anhui University, Hefei, Anhui 230601, China;2. Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui 230601, China;3. Department of Chemistry & Biochemistry, Florida International University, Miami, FL 33199, United States;1. Department of Bioscience and Food Production Science, Interdisciplinary Graduate School of Science and Technology, Shinshu University, 8304, Minami-minowa, Nagano, 399-4598, Japan;2. Faculty of Science, Srinakharinwirot University, 114, Sukhumvit 23, Bangkok, 10110, Thailand;3. Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University, 8304, Minami-minowa, Nagano, 399-4598, Japan;4. Division of Science, Faculty of Liberal Arts and Science, Nakhon Phanom University, 167 Naratchakouy Sub-District, Muang District, Nakhon Phanom, 48000, Thailand;5. Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwake-cho, Sakyo-ku, Kyoto, 606-8502, Japan;6. Division of Terrestrial Ecosystem, Institute of Mountain Science, Shinshu University, 8304, Minami-minowa, Nagano, 399-4598, Japan;1. State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People’s Republic of China;2. School of Marine Science and Technology, Jiangsu Marine Resources Development Research Institute, Huaihai Institute of Technology, Lianyungang, Jiangsu Province 222005, People’s Republic of China;1. Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama, 351-0198, Japan;2. Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka, 560-0043, Japan |
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| Abstract: | The intracellular galactose oxidase from Dactylium dendroides was purified to homogeneity with a 64% yield. The enzyme is a glycoprotein (7.7% neutral sugars, 1.7% aminosugars) with 72,000 Da of molecular mass. The enzyme showed nonlinear double reciprocal plots with O2 and D-galactose, suggesting cooperative binding for both substrates. The intracellular galactose oxidase catalyzes the oxidation of galactose derivatives and dihydroxyacetone but not of glycerol, glycolaldehyde, beta-hydroxipyruvate, and allyl alcohol which are substrates for the extracellular enzyme. Compared with the extracellular galactose oxidase, the intracellular enzyme showed higher carbohydrate content and sensitivity to diethyldithiocarbamate. |
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