Enzymatic Production of trans-4-Hydroxy-L-proline by Regio- and Stereospecific Hydroxylation of L-Proline
スポンサーリンク
概要
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A proline 4-hydroxylase gene, which was cloned from Dactylosporangium sp. RH1,was overexpressed in Escherichia coil W1485 on a plasmid under a tryptophan tandem promoter after the codon usage of the 5' end of the gene was optimized. The proline 4-hydroxylase activity was 1600-fold higher than that in Dactylosporangium sp. RH1. trans-4-Hydroxy-L-proline(Hyp) was produced and accumulated to 41g/L (87% yield from L-proline) in 100 h when the recombinant E. coli was cultivated in a medium containing L-proline and glucose. 2-Oxoglutarate, which is necessary for the hydroxylation of L-proline by proline 4-hydroxylase, was apparently supplied from glucose through the cellular metabolic pathway. The putA mutant of W1485,which is not able to degrade L-proline, has allowed the quantitative conversion of L-proline to Hyp. The formation of other isomers of hydroxyproline was not observed. Productivity of Hyp was almost the same in a largerscale culture. The method of manufacturing Hyp from L-proline was established.
- 社団法人日本農芸化学会の論文
- 2000-04-23
著者
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Mori H
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Mori Hironori
Department Of Biotechnology Faculty Of Agriculture The University Of Tokyo
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Ozaki A
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Ozaki Akio
Technical Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Ozaki Akio
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.:(present Office)technical Research Laboratori
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MORI HIDEO
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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SHIBASAKI Takeshi
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd.
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Shibasaki Takeshi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.: (present Address) Technical Research Laborat
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