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公开(公告)号:US4443548A
公开(公告)日:1984-04-17
申请号:US376236
申请日:1982-05-07
申请人: Tokio Oshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
发明人: Tokio Oshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
IPC分类号: C12P13/02 , C12N9/80 , C12P13/04 , C12P41/00 , C12R1/01 , C12R1/06 , C12R1/07 , C12R1/32 , C12R1/365 , C12R1/38 , C12R1/465 , C12R1/645 , C12R1/72 , C12R1/78 , C12R1/845 , C12R1/88 , C12R1/885 , C07B19/02 , C12P13/22
摘要: Biochemical optical resolution of DL-.alpha.-methylphenyl alanines in which DL-.alpha.-methylphenyl alanine amides are interacted with the culture products, or their treated products, of a microorganism capable of producing amidase is described. L-.alpha.-methylphenyl alanines having the general formula (I): ##STR1## wherein R.sub.1 and R.sub.2 may be independently a hydrogen atom or lower alkyl groups, or R.sub.1 and R.sub.2 may be alkylene groups combined together to form 5 through 8-membered rings is produced by the steps of:(a) making a DL-.alpha.-methylphenyl alanine amide having the general formula (II): ##STR2## wherein R.sub.1 and R.sub.2 are the same as defined above, interact with the culture product of a microorganism capable of producing enzyme catalyzing the hydrolysis of L-isomer of DL-.alpha.-methylphenyl alanine amides or the treated product thereof, whereby asymmetric hydrolysis of an L-.alpha.-methylphenyl alanine amide is effected; and(b) separating the resultant L-.alpha.-methylphenyl alanines from the hydrolysis mixture.
摘要翻译: 描述了DL-α-甲基苯丙氨酰胺与能够产生酰胺酶的微生物或其处理产物相互作用的DL-α-甲基苯基丙氨酸的生物化学光学拆分。 具有通式(I)的L-α-甲基苯基丙氨酸:其中R 1和R 2可以独立地为氢原子或低级烷基,或者R 1和R 2可以是亚烷基结合在一起形成5至8个 通过以下步骤制备环状环:(a)制备具有通式(II)的DL-α-甲基苯基丙氨酸酰胺:其中R 1和R 2与上述定义相同,与 能够产生催化DL-α-甲基苯丙氨酸酰胺的L-异构体或其处理产物的水解的酶的微生物的培养产物,从而实现了L-α-甲基苯丙氨酸酰胺的不对称水解; 和(b)从水解混合物中分离所得的L-α-甲基苯基丙氨酸。
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公开(公告)号:US4481362A
公开(公告)日:1984-11-06
申请号:US494692
申请日:1983-05-17
申请人: Mamoru Nakai , Tokio Ohshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
发明人: Mamoru Nakai , Tokio Ohshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
IPC分类号: C12N9/80 , C12P13/04 , C12P13/22 , C12P41/00 , C12R1/025 , C12R1/05 , C12R1/06 , C12R1/07 , C12R1/13 , C12R1/145 , C12R1/20 , C12R1/225 , C12R1/265 , C12R1/32 , C12R1/365 , C12R1/38 , C12R1/46 , C12R1/465 , C12R1/645 , C12R1/65 , C12R1/66 , C12R1/72 , C12R1/77 , C12R1/78 , C12R1/80 , C12R1/84 , C12R1/845 , C12R1/85 , C12R1/88 , C12R1/885 , C07D209/20
CPC分类号: C12N9/80 , C12P13/04 , C12P13/227
摘要: Biochemical optical resolution of DL-tryptophanes in which DL-tryptophane amides are interacted with the culture products, or their treated products, of a microorganism capable of producing amidase is described. L-tryptophane amides in racemic DL-tryptophane amides are asymmetrically hydrolyzed to form optically active L-tryptophanes at a high yield and almost all D-tryptophane amides remain without being subjected to hydrolysis. The resultant D-tryptophane amides are readily hydrolyzed, after separating L-tryptophanes, to form optically active D-tryptophanes at a high yield.
摘要翻译: 描述DL-色氨酰胺与能够产生酰胺酶的微生物或其处理产物相互作用的DL-色氨酸的生物化学光学拆分。 外消旋的DL-色氨酰胺中的L-色氨酰胺不对称地水解,以高产率形成光学活性的L-色氨酸,并且几乎所有的D-色氨酸酰胺保持不被水解。 得到的D-色氨酰胺在分离L-色氨酸后容易水解,以高产率形成光学活性的D-色氨酸。
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公开(公告)号:US4497957A
公开(公告)日:1985-02-05
申请号:US391997
申请日:1982-06-25
申请人: Mamoru Nakai , Tokio Ohshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
发明人: Mamoru Nakai , Tokio Ohshima , Tomio Kimura , Tetsuo Omata , Noritada Iwamoto
IPC分类号: C12N9/80 , C12P13/04 , C12P13/22 , C12P41/00 , C12R1/025 , C12R1/05 , C12R1/06 , C12R1/07 , C12R1/13 , C12R1/145 , C12R1/20 , C12R1/225 , C12R1/265 , C12R1/32 , C12R1/365 , C12R1/38 , C12R1/46 , C12R1/465 , C12R1/645 , C12R1/65 , C12R1/66 , C12R1/72 , C12R1/77 , C12R1/78 , C12R1/80 , C12R1/84 , C12R1/845 , C12R1/85 , C12R1/88 , C12R1/885 , C07D209/20
CPC分类号: C12N9/80 , C12P13/04 , C12P13/227
摘要: Biochemical optical resolution of DL-tryptophans in which DL-tryptophan amides are interacted with the culture products, or their treated products, of a microorganism capable of producing amidase is described. L-Tryptophan amides in racemic DL-tryptophan amides are asymmetrically hydrolyzed to form optically active L-tryptophans at a high yield and almost all D-tryptophan amides remain without being subjected to hydrolysis. The resultant D-tryptophan amides are readily hydrolyzed, after separating L-tryptophans, to form optically active D-tryptophans at a high yield.
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