Purification and Characterization of Acyl Coenzyme A: Alcohol Acyltransferase of Neurospora sp.(Biological Chemistry)
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概要
- 論文の詳細を見る
Acyl coenzyme A: alcohol acyltransferase was purified to homogeneity from a strain of Neurospora sp. ATCC 46892 which produces ethyl hexanoate abundantly in the culture broth. The apparent molecular weight was approximately 30,000. This enzyme acted on various acyl coenzyme A's containing more than a four-carbon linear chain, but not on acetyl coenzyme A, n-propionyl coenzyme A, or the branched-chain acyl coenzyme A's that were examined. It also acted on various linear- and branched-chain alcohols tested. The optimum pH was 8.0, and the optimum temperature, 25℃ at pH 8.0. The enzyme was stable from pH 3.0 to 9.0 and up to 43℃, maintaining its original activity. The enzyme activity was strongly inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride, but not by unsaturated fatty acids.
- 社団法人日本農芸化学会の論文
- 1989-06-23
著者
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AKITA Osamu
National Research Institute of Brewing (NRIB)
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HARA Shodo
National Research Institute of Brewing
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YOSHIZAWA Kiyoshi
National Research Institute of Brewing
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AMACHI Teruo
Laboratories of Applied Microbiology, Research Center, Suntory Ltd.
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Hara S
General Research Laboratory Of Kiku-masamune Sake Brewing Co. Ltd.
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Akita O
Fac. Of Human Life Sciences Dep. Of Food And Health Sciences Jissen Women's Univ.
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Akita Osamu
National Research Institute Of Brewing
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Amachi T
Kyoto Univ. Kyoto Jpn
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Yamauchi H
Marutomo Co. Ltd. Ehime Jpn
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YAMAUCHI Hiromasa
National Research Institute of Brewing
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HASUO Tetsuo
National Research Institute of Brewing
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Yoshizawa K
Tokyo Univ. Agriculture Tokyo Jpn
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