Purification and Properties of Five NADP-dependent Aldehyde Dehydrogenases from Acetobacter aceti
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概要
- 論文の詳細を見る
Five aldehyde dehydrogenases were purified from the cell-free extract of Acetobacter aceti and designated aldehyde dehydrogenases a, b, c, d and e. All of them were monomer enzymes and their molecular weights were as follows : a, 65,000; b, 82,000; c, 58,000; d, 87,000; e, 70,000.These enzymes resembled those of A. suboxydans, of yeast and those of mammalian origins in various respects. All the enzymes showed pH optima between 4.5 and 9.They were stable at a pH range of 8 to 9,but were unstable at an acidic pH of under 4. All the enzymes showed very broad substrate specificities to aliphatic n-mono-aldehydes.
- 公益社団法人日本生物工学会の論文
- 1980-12-25
著者
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TAKAHASHI Hajime
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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Ogasawara Nagahiro
Department Of Agricultural Chemistry Niigata University
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Ogasawara Nagahiro
Department Of Agricultural Chemistry Faculty Of Agriculture Niigata Unirersity
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MURAOKA HIROSHI
Fukushima Factory, Kikko Foods Ind. Co.,
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WATABE YOSHIMI
Fukushima Factory, Kikko Foods Ind. Co.,
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Watabe Yoshimi
Fukushima Factory Kikko Foods Ind. Co.
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Muraoka Hiroshi
Fukushima Factory Kikko Foods Ind. Co.
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Takahashi Hajime
Department Of Agricultural Chemistry Tohoku University
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Takahashi Hajime
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Takahashi Hajime
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku Uleiversity
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