Crystallization and Some Properties of D-Lactate Dehydrogenase from Staphylococcus sp. LDH-1
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概要
- 論文の詳細を見る
Staphylococcus sp. LDH-1 isolated as a high producer of lactate dehydrogenase grew well under anaerobic conditions and produced a large amount of D-lactate dehydrogenase (D-LDH), but not L-LDH. After purification of this D-LDH, some properties were revealed. The enzyme catalyzed the reversible reduction of 2-oxo acids into D-2-hydroxy acids, but not into L-2-hydroxy acids. The K_m values for 2-oxo acids were much smaller than those for D-2-hydroxy acids, and the Vmax values for 2-oxo acids were much greater than those for D-2-hydroxy acids. The equilibrium constants for the reaction of the reductions of pyruvic acid to D-lactic acid and of 2-oxobutyric acid to D-2-hydroxy-n-butyric acid were 270 and 360, respectively. The enzyme was stable between pH5.5 and 8.5, while the optimum pH for pyruvic acid and D-lactic acid was pH5.0 and 8.2, respectively. It was therefore concluded that the D-LDH from Staphylococcus sp. LDH-1 is available as enzyme for an assay of pyruvic acid and for the production of D-2-hydroxy acids.
- 社団法人日本生物工学会の論文
- 2002-10-25
著者
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Isobe Kimiyasu
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
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Isobe K
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Isobe Kimiyasu
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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YOKOE MASAAKI
Gifu Research and Development Center, Amano Enzyme Inc.
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WAKAO NORIO
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
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KOIDE YOSHINAO
Gifu Research and Development Center, Amano Enzyme Inc.
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Wakao Norio
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Wakao N
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Yokoe Masaaki
Gifu Research And Development Center Amano Enzyme Inc.
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Koide Yoshinao
Gifu Research And Development Center Amano Enzyme Inc.
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