Lipase-catalyzed ring-opening polymerization of 16-hexadecanolide
スポンサーリンク
概要
- 論文の詳細を見る
Enzymatic ring-opening polymerization of a 17-membered lactone, 16-hexadecanolide (HDL), was performed in bulk by using lipases of different origin as catalyst. Pseudomonas fluorescens lipase exhibited high catalytic activity toward the polymerization, producing the corresponding polymer in high yields. A higher polymerization temperature (75°C) resulted in the formation of the polymer with molecular weight of more than 5×103. HDL monomer was recovered unchanged in the polymerization without the enzyme. Michaelis-Menten kinetics of lactones in five different ring size showed that HDL had the largest enzymatic polymerizability among the lactones examined.
- 日本学士院の論文
著者
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UYAMA Hiroshi
Department of Applied Chemistry, Graduate School of Engineering, Osaka University
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宇山 浩
大阪大学工学研究科応用化学専攻
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宇山 浩
大阪大学大学院工学研究科応用化学専攻
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KOBAYASHI Shiro
Department of Neurosurgery, Chiba Hokusoh Hospital, Nippon Medical School
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宇山 浩
大阪大学
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NAMEKAWA Shuhei
Department of Materials Chemistry, Graduate School of Engineering, Tohoku University
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Uyama Hiroshi
Department Of Applied Chemistry Graduate School Of Engineering Osaka University
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Kobayashi S
Department Of Materials Chemistry Graduate School Of Engineering Kyoto University
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Namekawa S
Tohoku Univ. Sendai Jpn
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Namekawa Shuhei
Department Of Materials Chemistry Graduate School Of Enginnering Tohoku University
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Kobayashi Shiro
Department Of Neurosurgery Chiba Hokuso Hospital Nippon Medical School
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Kobayashi Shiro
Department Of Material Chemistry Graduate School Of Engineering Kyoto University
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