High Level Expression of XMP Aminase in Escherichia coli and Its Application for the Industrial Production of 5'-Guanylic Acid
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概要
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To improve the efficiency of the enzymatic conversion of 5'-xanthylic acid (XMP) to 5'-guanylic acid (GMP), we attempted to increase the activity of the conversion enzyme, XMP aminase (GMP synthetase) encoded by the guaA gene in Escherichia coli. By connecting the P_L promoter of λ phage, the SD sequence of trpL of E. coli, and ATG, at a suitable position upstream of the guaA gene, we obtained plasmid pPLA66. Sequencing of the nucleotides of the upstream region of the guaA gene on pPLA66 showed that the C-terminal region of the guaB gene, which encodes IMP dehydrogenase, was conserved and a short peptide consisted of 14 amino acids was coded. E. coli MP347/pPLA66 showed an increase in the activity of approximately 370 times when compared with that of the strain MM294, and the amount of the enzyme protein represented approx. 34% of the total cellular protein. Strain MP347/pPLA66 was cultivated in a 5-liter jar fermentor using a medium which contained mainly corn steep liquor. The culture broth had high XMP aminase activity. In the conversion reaction using mixed broths consisted of 600ml of XMP-fermentation broth of Corynebacterium ammoniagenes KY13203 and 30ml of cultured broth of E. coli MP347/pPLA66, a surfactant, Nymeen S-215 and xylene were added to the reaction mixture to make the cell membrane permeable to nucleotides. After 23h of the reaction, 70mg/ml (131mM) of GMP・Na_2・7H_2O was accumulated from 83 mg/ml (155 mM) of XMP・Na_3.7H_2O, without addition of ATP. The molar conversion yield was approx. 85%. The facts that the cell membrane was treated to allow nucleotides to permeate and that the conversion reaction proceeded well enough in spite of a small amount of E. coli cells indicate ATP was regenerated from AMP by C. ammoniagenes cells and supplied to E. coli cells. Therefore, it was considered that the coupling reaction between these two kind of strains was established.
- 社団法人日本農芸化学会の論文
- 1997-05-23
著者
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Ito S
Extremobiosphere Research Center Of Japan Agency For Marine-earth Science And Technology (jamstec):c
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NISHI Tatsunari
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd.
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Maruyama Akihiko
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Maruyama Akihiko
Fine Chemicals Biochemicals Dept. Medicals Research And Development Center Kyowa Hakko Kogyo Co. Ltd
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Maruyama Akihiko
Fine Chemicals
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Maruyama Akihiko
(present Address) Fermentation Research Institute Agency Of Industrial Science And Technology
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Ito S
National Industrial Research Institute
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Sugimoto Isamu
Division Of Pathological Biochemistry Department Of Biomedical Sciences School Of Life Sciences Facu
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FUJIO Tatsuro
Planning & Development Department
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Fujio T
Kyowa Hakko Kogyo Co. Ltd. Tokyo Jpn
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ITO Seiga
Pharmaceutical Research Laboratories, Kyowa Hakko Kogyo Co., Ltd.
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Nishi T
Hokkaido Univ. Sapporo Jpn
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Nishi Tatsunari
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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