Preparative asymmetric reduction of ketones in a biphasic medium with an (S)-alcohol dehydrogenase under in situ-cofactor-recycling with a formate dehydrogenase

Tetrahedron

Volumn 60, Issue 3, 2004, Pages 633-640

  Gröger, Harald ^a   Hummel, Werner ^b   Rollmann, Claudia ^a   Chamouleau, Francoise ^a   Hüsken, Hendrik ^a   Werner, Helge ^a   Wunderlich, Christine ^a   Abokitse, Kofi ^b   Drauz, Karlheinz ^a   Buchholz, Stefan ^a  

^a EVONIK INDUSTRIES AG   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

(S) Alcohol; In situ cofactor regeneration; Ketones

Indexed keywords

ACETOPHENONE; ALCOHOL DEHYDROGENASE; BACTERIAL ENZYME; FORMATE DEHYDROGENASE; FUNGAL ENZYME; KETONE; WATER;

ARTICLE; BIOCATALYST; CANDIDA BOIDINII; CHEMICAL REACTION; CONCENTRATION (PARAMETERS); ENZYME ACTIVITY; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RECYCLING; REDUCTION; RHODOCOCCUS ERYTHROPOLIS;

CANDIDA BOIDINII; ERYTHROPOLIS; RHODOCOCCUS ERYTHROPOLIS;

EID: 0346964416     PISSN: 00404020     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tet.2003.11.066     Document Type: Article

References (40)

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6. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
7. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
8. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
9. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
10. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
11. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
12. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
13. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
14. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
15. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
16. Numerous efficient (S)- and (R)-specific alcohol dehydrogenases have been already found. For selected contributions, see: (a) Bradshaw C.W., Hummel W., Wong C.-H. J. Org. Chem. 57:1992;1532 (b) Ammendola S., Raia C.A., Caruso C., Camardella L., D'Auria S., De Rosa M., Rossi M. Biochemistry. 31:1992;12514-12523 (c) Cannio R., Fiorentino G., Carpinelli P., Rossi M., Bartolucci S. J. Bacteriol. 178:1996;301-305 (d) Bogin O., Peretz M., Burstein Y. Protein Sci. 6:1997;450-458 (e) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (f) Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C. FEMS Microbiol. Lett. 190:2000;57-62 (g) Matsuda T., Harada T., Nakamura K. Chem. Commun. 2000;1367-1368 (h) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (i) Schubert T., Hummel W., Kula M.-R., Müller M. Eur. J. Org. Chem. 2001;4181-4187 (j) Stampfer W., Kosjek B., Moitzi C., Kroutil W., Faber K. Angew. Chem. 114:2002;1056-1059 (k) Abokitse K., Hummel W. Appl. Microbiol. Biotechnol. 62:2003;380-386.
17. For reviews about biocatalytic reductions in general, see: (a) Hummel W. Adv. Biochem. Engng Biotechnol. 58:1997;146-184 (b) Faber K. Biotransformations in organic chemistry. 4th ed. 2000;Springer, Berlin. Chapter 2.2.3, pp 192-194.
18. For reviews about biocatalytic reductions in general, see: (a) Hummel W. Adv. Biochem. Engng Biotechnol. 58:1997;146-184 (b) Faber K. Biotransformations in organic chemistry. 4th ed. 2000;Springer, Berlin. Chapter 2.2.3, pp 192-194.
19. For selected contributions of an alternative approach via asymmetric metal-catalyzed hydrogenation of ketones, see: (a) Burk M.J., Hems W., Herzberg D., Malan C., Zanotti-Gerosa A. Org. Lett. 2:2000;4173-4176 (b) Ohkuma T., Koizumi M., Yoshida M., Noyori R. Org. Lett. 2:2000;1749-1751 (c) Ohkuma T., Takeno H., Honda Y., Noyori R. Adv. Synth. Catal. 343:2001;369-375. Review: (d) Noyori R., Okhuma T. Angew. Chem., Int. Ed. 40:2001;40-73.
20. For selected contributions of an alternative approach via asymmetric metal-catalyzed hydrogenation of ketones, see: (a) Burk M.J., Hems W., Herzberg D., Malan C., Zanotti-Gerosa A. Org. Lett. 2:2000;4173-4176 (b) Ohkuma T., Koizumi M., Yoshida M., Noyori R. Org. Lett. 2:2000;1749-1751 (c) Ohkuma T., Takeno H., Honda Y., Noyori R. Adv. Synth. Catal. 343:2001;369-375. Review: (d) Noyori R., Okhuma T. Angew. Chem., Int. Ed. 40:2001;40-73.
21. For selected contributions of an alternative approach via asymmetric metal-catalyzed hydrogenation of ketones, see: (a) Burk M.J., Hems W., Herzberg D., Malan C., Zanotti-Gerosa A. Org. Lett. 2:2000;4173-4176 (b) Ohkuma T., Koizumi M., Yoshida M., Noyori R. Org. Lett. 2:2000;1749-1751 (c) Ohkuma T., Takeno H., Honda Y., Noyori R. Adv. Synth. Catal. 343:2001;369-375. Review: (d) Noyori R., Okhuma T. Angew. Chem., Int. Ed. 40:2001;40-73.
22. For selected contributions of an alternative approach via asymmetric metal-catalyzed hydrogenation of ketones, see: (a) Burk M.J., Hems W., Herzberg D., Malan C., Zanotti-Gerosa A. Org. Lett. 2:2000;4173-4176 (b) Ohkuma T., Koizumi M., Yoshida M., Noyori R. Org. Lett. 2:2000;1749-1751 (c) Ohkuma T., Takeno H., Honda Y., Noyori R. Adv. Synth. Catal. 343:2001;369-375. Review: (d) Noyori R., Okhuma T. Angew. Chem., Int. Ed. 40:2001;40-73.
23. For selected contributions of an alternative approach via asymmetric whole-cell-biocatalytic reduction of ketones, see: (a) Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Tetrahedron: Asymmetry. 12:2001;1713-1718 (b) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (c) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (d) Stampfer W., Kosjek B., Faber K., Kroutil W. J. Org. Chem. 68:2003;402-406 (e) Haberland J., Hummel W., Dauβmann T., Liese A. Org. Proc. Res. Dev. 6:2002;458-462.
24. For selected contributions of an alternative approach via asymmetric whole-cell-biocatalytic reduction of ketones, see: (a) Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Tetrahedron: Asymmetry. 12:2001;1713-1718 (b) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (c) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (d) Stampfer W., Kosjek B., Faber K., Kroutil W. J. Org. Chem. 68:2003;402-406 (e) Haberland J., Hummel W., Dauβmann T., Liese A. Org. Proc. Res. Dev. 6:2002;458-462.
25. For selected contributions of an alternative approach via asymmetric whole-cell-biocatalytic reduction of ketones, see: (a) Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Tetrahedron: Asymmetry. 12:2001;1713-1718 (b) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (c) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (d) Stampfer W., Kosjek B., Faber K., Kroutil W. J. Org. Chem. 68:2003;402-406 (e) Haberland J., Hummel W., Dauβmann T., Liese A. Org. Proc. Res. Dev. 6:2002;458-462.
26. For selected contributions of an alternative approach via asymmetric whole-cell-biocatalytic reduction of ketones, see: (a) Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Tetrahedron: Asymmetry. 12:2001;1713-1718 (b) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (c) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (d) Stampfer W., Kosjek B., Faber K., Kroutil W. J. Org. Chem. 68:2003;402-406 (e) Haberland J., Hummel W., Dauβmann T., Liese A. Org. Proc. Res. Dev. 6:2002;458-462.
27. For selected contributions of an alternative approach via asymmetric whole-cell-biocatalytic reduction of ketones, see: (a) Yasohara Y., Kizaki N., Hasegawa J., Wada M., Kataoka M., Shimizu S. Tetrahedron: Asymmetry. 12:2001;1713-1718 (b) Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:1998;967-981 (c) Riebel B., Hummel W. Biotechnol. Lett. 23:2001;231-234 (d) Stampfer W., Kosjek B., Faber K., Kroutil W. J. Org. Chem. 68:2003;402-406 (e) Haberland J., Hummel W., Daumann T., Liese A. Org. Proc. Res. Dev. 6:2002;458-462.
28. For selected contributions of an alternative approach via asymmetric reduction of ketones based on substrate-coupled cofactor-regeneration, see: (a) Wolberg M., Ji A.G., Hummel W., Müller M. Synthesis. 2001;937-942 (b) Schubert T., Hummel W., Müller M. Angew. Chem. 114:2002;656-659 (c) Stillger T., Bönitz M., Villela F., Liese A. Chem. Ing. Techn. 74:2002;1035-1039.
29. For selected contributions of an alternative approach via asymmetric reduction of ketones based on substrate-coupled cofactor-regeneration, see: (a) Wolberg M., Ji A.G., Hummel W., Müller M. Synthesis. 2001;937-942 (b) Schubert T., Hummel W., Müller M. Angew. Chem. 114:2002;656-659 (c) Stillger T., Bönitz M., Villela F., Liese A. Chem. Ing. Techn. 74:2002;1035-1039.
30. For selected contributions of an alternative approach via asymmetric reduction of ketones based on substrate-coupled cofactor-regeneration, see: (a) Wolberg M., Ji A.G., Hummel W., Müller M. Synthesis. 2001;937-942 (b) Schubert T., Hummel W., Müller M. Angew. Chem. 114:2002;656-659 (c) Stillger T., Bönitz M., Villela F., Liese A. Chem. Ing. Techn. 74:2002;1035-1039.
31. The properties of the cofactor-regenerating enzyme FDH from C. boidinii have been improved remarkably by protein engineering in the Kula group. Thus, a stable and efficient formate dehydrogenase is now available on large scale for NADH-regeneration, see: Slusarczyk H., Felber S., Kula M.-R., Pohl M. Eur. J. Biochem. 267:2000;1280-1289.
32. In spite of its high technical potential and applicability, the FDH from C. boidinii was found to be sensitive towards the presence of organic solvents. The general problem of rapid deactivation of enzymes other than hydrolases in the presence of organic solvents, has been previously described in several coontributions, e.g. in: Kruse, W.; Kragl, U.; Wandrey, C. DE 4436149, 1996.
33. This efficient 'three-loops'-concept is based on an enzymatic reaction in pure aqueous medium, a separation of the aqueous phase from the enzyme via ultrafiltration, and a subsequent continuous extraction of the aqueous phase with an organic solvent. Organic and aqueous phases are separated by a hydrophobic membrane. This method is described in: (a) Liese A., Seelbach K., Wandrey C. Industrial biotransformations. 2000; Wiley-VCH, Weinheim, (b) Kruse W., Hummel W., Kragl U. Recl. Trav. Chim. Pays-Bas. 115:1996;239-243.
34. This efficient 'three-loops'-concept is based on an enzymatic reaction in pure aqueous medium, a separation of the aqueous phase from the enzyme via ultrafiltration, and a subsequent continuous extraction of the aqueous phase with an organic solvent. Organic and aqueous phases are separated by a hydrophobic membrane. This method is described in: (a) Liese A., Seelbach K., Wandrey C. Industrial biotransformations. 2000; Wiley-VCH, Weinheim, (b) Kruse W., Hummel W., Kragl U. Recl. Trav. Chim. Pays-Bas. 115:1996;239-243.
35. For preliminary communications, see: (a) Hummel W., Abokitse K., Drauz K., Rollmann C., Gröger H. Adv. Synth. Catal. 345:2003;153-159 (b) Gröger H., Hummel W., Buchholz S., Drauz K., Nguyen T.V., Rollmann C., Hüsken H., Abokitse K. Org. Lett. 5:2003;173-176.
36. For preliminary communications, see: (a) Hummel W., Abokitse K., Drauz K., Rollmann C., Gröger H. Adv. Synth. Catal. 345:2003;153-159 (b) Gröger H., Hummel W., Buchholz S., Drauz K., Nguyen T.V., Rollmann C., Hüsken H., Abokitse K. Org. Lett. 5:2003;173-176.
37. (a) Hummel, W.; Gottwald, C. DOS 4209022, 1993; Chem. Abstr. 1994, 120, 29495.
38. (b) Zelinski T., Peters J., Kula M.-R. J. Biotechnol. 33:1994;283-292.
39. The determination of enzyme activities were done using a cell-free crude extract of E. coli with the recombinant (S)-ADH enzyme from R. erythropolis. In addition, activity studies were also done with a (partially) purified form of the enzyme. The presence of other dehydrogenases causing a background activity was not observed in the experimental investigation. The specific activities of this (S)-ADH from R. erythropolis expressed in E. coli is in the range of 100-1000 U/mg of purified protein depending of the structure to be converted, see also Ref. 3k. For comparison, horse liver alcohol dehydrogenase as one of the most widely applied (S)-alcohol dehydrogenase so far shows an activity in the range of 1-3 U/mg only, see Ref. 1a.
40. It is to be noticed that several differences in substrate range were observed in comparison with the corresponding wild-type alcohol dehydrogenases (from crude extracts), see also Ref. 11a.