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Volumn 38, Issue 1-2, 2006, Pages 126-134

Use of a UF-membrane reactor for controlling selectively the nitrile hydratase-amidase system in Microbacterium imperiale CBS 498-74 resting cells - Case study: Benzonitrile conversion

Author keywords

Benzonitrile biotransformation; Enzyme kinetics; Microbacterium imperiale; Nitrile hydratase amidase system; UF membrane reactor

Indexed keywords

BACTERIA; BIOREACTORS; CELLS; ENZYME KINETICS; MEMBRANES; ULTRAFILTRATION;

EID: 27844483915     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.05.002     Document Type: Article
Times cited : (28)

References (36)
  • 2
    • 0041692758 scopus 로고    scopus 로고
    • Synthetic applications of nitrile-converting enzymes
    • V. Mylerova, and L. Martinkova Synthetic applications of nitrile-converting enzymes Curr Org Chem 7 2003 1 17
    • (2003) Curr Org Chem , vol.7 , pp. 1-17
    • Mylerova, V.1    Martinkova, L.2
  • 3
    • 0035313673 scopus 로고    scopus 로고
    • Industrial biocatalysis
    • A. Zaks Industrial biocatalysis Curr Opin Chem Biol 5 2001 130 136
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 130-136
    • Zaks, A.1
  • 5
    • 0001055519 scopus 로고
    • Microbial production of commodity chemicals
    • T. Nagasawa, and H. Yamada Microbial production of commodity chemicals Pure Appl Chem 67 1995 1241 1256
    • (1995) Pure Appl Chem , vol.67 , pp. 1241-1256
    • Nagasawa, T.1    Yamada, H.2
  • 6
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial-production of acrylamide
    • H. Yamada, and M. Kobayashi Nitrile hydratase and its application to industrial-production of acrylamide Biosci Biotechnol Biochem 60 1996 1391 1400
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 7
    • 0031879561 scopus 로고    scopus 로고
    • Metalloenzyme nitrile hydratase: Structure, regulation and application to biotechnology
    • M. Kobayashi, and S. Shimizu Metalloenzyme nitrile hydratase: structure, regulation and application to biotechnology Nat Biotechnol 16 1998 733 736
    • (1998) Nat Biotechnol , vol.16 , pp. 733-736
    • Kobayashi, M.1    Shimizu, S.2
  • 10
    • 0029311323 scopus 로고
    • The development of a novel strategy for the microbial treatment of acrylonitrile effluents
    • J.M. Wyatt, and C.J. Knowles The development of a novel strategy for the microbial treatment of acrylonitrile effluents Biodegradation 6 1995 93 107
    • (1995) Biodegradation , vol.6 , pp. 93-107
    • Wyatt, J.M.1    Knowles, C.J.2
  • 11
    • 0030894383 scopus 로고    scopus 로고
    • Enzymatic decontamination of aqueous polymer emulsions containing acrylonitrile
    • E. Battistel, A. Bernardi, and P. Maestri Enzymatic decontamination of aqueous polymer emulsions containing acrylonitrile Biotechnol Lett 19 1997 131 134
    • (1997) Biotechnol Lett , vol.19 , pp. 131-134
    • Battistel, E.1    Bernardi, A.2    Maestri, P.3
  • 12
    • 0001093905 scopus 로고    scopus 로고
    • Biocatalysis in organic-synthesis. the use of nitrile-hydrolyzing and amide-hydrolyzing microorganisms
    • T. Sugai, T. Yamazaki, M. Yokoyama, and H. Ohta Biocatalysis in organic-synthesis. The use of nitrile-hydrolyzing and amide-hydrolyzing microorganisms Biosci Biotechnol Biochem 61 1997 1419 1427
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1419-1427
    • Sugai, T.1    Yamazaki, T.2    Yokoyama, M.3    Ohta, H.4
  • 13
    • 33749110448 scopus 로고    scopus 로고
    • An in-depth study of the biotransformations of nitriles into amides and/or acids using Rhodococcus rhodochrous AJ270
    • O. Meth-Cohn, and M.X. Wang An in-depth study of the biotransformations of nitriles into amides and/or acids using Rhodococcus rhodochrous AJ270 J Chem Soc Perkin Trans 1 1997 1099 1104
    • (1997) J Chem Soc Perkin Trans , vol.1 , pp. 1099-1104
    • Meth-Cohn, O.1    Wang, M.X.2
  • 14
    • 0037375238 scopus 로고    scopus 로고
    • Biocatalytic asymmetric hydrolysis of (±)-β-hydroxynitriles by Rhodococcus sp. CGMCC 0497
    • Z.L. Wu, and Z.Y. Li Biocatalytic asymmetric hydrolysis of (±)-β-hydroxynitriles by Rhodococcus sp. CGMCC 0497 J Mol Catal B Enzymatic 22 2003 105 112
    • (2003) J Mol Catal B Enzymatic , vol.22 , pp. 105-112
    • Wu, Z.L.1    Li, Z.Y.2
  • 15
    • 0032953196 scopus 로고    scopus 로고
    • Transcriptional analysis of the nitrile-degrading operon from Rhodococcus sp. ACV2 and high level production of recombinant amidase with an Escherichia coli-T7 expression system
    • F. Bigey, H. Chebrou, D. Fournand, and A. Arnaud Transcriptional analysis of the nitrile-degrading operon from Rhodococcus sp. ACV2 and high level production of recombinant amidase with an Escherichia coli-T7 expression system J Appl Microbiol 86 1999 752 760
    • (1999) J Appl Microbiol , vol.86 , pp. 752-760
    • Bigey, F.1    Chebrou, H.2    Fournand, D.3    Arnaud, A.4
  • 16
    • 0345084461 scopus 로고    scopus 로고
    • Chemo- and enantioselective hydrolysis of nitriles and acid amides, respectively, with resting cells of Rhodococcus sp. C3II and Rhodococcus erythropolis MP50
    • F. Effenberger, and B.W. Graef Chemo- and enantioselective hydrolysis of nitriles and acid amides, respectively, with resting cells of Rhodococcus sp. C3II and Rhodococcus erythropolis MP50 J Biotechnol 60 1998 165 174
    • (1998) J Biotechnol , vol.60 , pp. 165-174
    • Effenberger, F.1    Graef, B.W.2
  • 17
    • 37049083979 scopus 로고
    • Regioselective hydrolysis of aromatic dinitriles using a whole cell catalyst
    • J. Crosby, J. Moiliet, J.S. Parratt, and N.J. Turner Regioselective hydrolysis of aromatic dinitriles using a whole cell catalyst J Chem Soc Perkin Trans 1 1994 1679 1687
    • (1994) J Chem Soc Perkin Trans , vol.1 , pp. 1679-1687
    • Crosby, J.1    Moiliet, J.2    Parratt, J.S.3    Turner, N.J.4
  • 18
    • 0036159384 scopus 로고    scopus 로고
    • Characterization and synthetic applications of recombinant AtNIT1 from Arabidopsis thaliana
    • S. Osswald, H. Wajant, and F. Effenberger Characterization and synthetic applications of recombinant AtNIT1 from Arabidopsis thaliana Eur J Biochem 269 2002 680 687
    • (2002) Eur J Biochem , vol.269 , pp. 680-687
    • Osswald, S.1    Wajant, H.2    Effenberger, F.3
  • 19
    • 0001713876 scopus 로고
    • Ricinine nitrilase. I. Reaction product and substrate specificity
    • W.G. Robinson, and R.H. Hook Ricinine nitrilase. I. Reaction product and substrate specificity J Biol Chem 239 1964 4257 4262
    • (1964) J Biol Chem , vol.239 , pp. 4257-4262
    • Robinson, W.G.1    Hook, R.H.2
  • 20
    • 0017191570 scopus 로고
    • Purification and properties of an unusual nitrilase from Nocardia NCIMB 11216
    • D. Harper Purification and properties of an unusual nitrilase from Nocardia NCIMB 11216 Biochem Soc Trans 4 1976 502 504
    • (1976) Biochem Soc Trans , vol.4 , pp. 502-504
    • Harper, D.1
  • 21
    • 0017393718 scopus 로고
    • Microbial metabolism of aromatic nitriles - Enzymology of C-N cleavage by Nocardia sp. (Rhodococcus group) NCIMB 11216
    • D. Harper Microbial metabolism of aromatic nitriles - enzymology of C-N cleavage by Nocardia sp. (Rhodococcus group) NCIMB 11216 Biochem J 165 1977 309 319
    • (1977) Biochem J , vol.165 , pp. 309-319
    • Harper, D.1
  • 22
    • 0000020934 scopus 로고
    • A new enzyme "nitrile hydratase" which degrades acetonitrile in combination with amidase
    • Y. Asano, Y. Tani, and H. Yamada A new enzyme "Nitrile hydratase" which degrades acetonitrile in combination with amidase Agric Biol Chem 44 1980 2251 2252
    • (1980) Agric Biol Chem , vol.44 , pp. 2251-2252
    • Asano, Y.1    Tani, Y.2    Yamada, H.3
  • 23
    • 0028289876 scopus 로고
    • Versatile nitrilases: Nitrile hydrolysing enzymes
    • M. Kobayashi, and S. Shimizu Versatile nitrilases: nitrile hydrolysing enzymes FEMS Microbiol Lett 120 1994 217 224
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 217-224
    • Kobayashi, M.1    Shimizu, S.2
  • 24
    • 0023118310 scopus 로고
    • Nitrile hydratase of Pseudomonas chlororaphis B23 purification and characterization
    • T. Nagasawa, H. Nanba, K. Ryuno, K. Takeuchi, and H. Yamada Nitrile hydratase of Pseudomonas chlororaphis B23 purification and characterization Eur J Biochem 162 1987 691 698
    • (1987) Eur J Biochem , vol.162 , pp. 691-698
    • Nagasawa, T.1    Nanba, H.2    Ryuno, K.3    Takeuchi, K.4    Yamada, H.5
  • 26
    • 84985257117 scopus 로고
    • Purification and characterization of nitrile hydratase of a mutant strain of Brevibacterium sp.
    • J.L. Moreau, S. Azza, A. Arnaud, and P. Galzy Purification and characterization of nitrile hydratase of a mutant strain of Brevibacterium sp. J Basic Microbiol 33 1993 323 329
    • (1993) J Basic Microbiol , vol.33 , pp. 323-329
    • Moreau, J.L.1    Azza, S.2    Arnaud, A.3    Galzy, P.4
  • 27
    • 0026169411 scopus 로고
    • Bioconversion of acrylonitrile into acrylamide using a highly compact multiphasic reactor
    • N. Bernet, P. Naouri, A. Arnaud, P. Galzy, and G.M. Rios Bioconversion of acrylonitrile into acrylamide using a highly compact multiphasic reactor Chem Eng J 46 1991 B43 B51
    • (1991) Chem Eng J , vol.46
    • Bernet, N.1    Naouri, P.2    Arnaud, A.3    Galzy, P.4    Rios, G.M.5
  • 28
    • 0027703822 scopus 로고
    • Bench-scale production of acrylamide using the resting cells of Brevibacterium sp. CH2 in a fed-batch reactor
    • C.Y. Lee, S.K. Choi, and H.N. Chang Bench-scale production of acrylamide using the resting cells of Brevibacterium sp. CH2 in a fed-batch reactor Enzyme Microb Technol 15 1993 979 984
    • (1993) Enzyme Microb Technol , vol.15 , pp. 979-984
    • Lee, C.Y.1    Choi, S.K.2    Chang, H.N.3
  • 29
    • 0037010701 scopus 로고    scopus 로고
    • Influence of initial glucose concentration on nitrile hydratase production in Brevibacterium imperialis CBS 498-74
    • M. Cantarella, A. Spera, P. Leonetti, and F. Alfani Influence of initial glucose concentration on nitrile hydratase production in Brevibacterium imperialis CBS 498-74 J Mol Catal B Enzymatic 19 2002 405 414
    • (2002) J Mol Catal B Enzymatic , vol.19 , pp. 405-414
    • Cantarella, M.1    Spera, A.2    Leonetti, P.3    Alfani, F.4
  • 30
    • 2442522450 scopus 로고    scopus 로고
    • A study in UF-membrane reactor on activity and stability of nitrile hydratase from Microbacterium imperiale CBS 498-74 resting cells for propioamide production
    • M. Cantarella, L. Cantarella, A. Gallifuoco, R. Frezzini, A. Spera, and F. Alfani A study in UF-membrane reactor on activity and stability of nitrile hydratase from Microbacterium imperiale CBS 498-74 resting cells for propioamide production J Mol Catal B Enzymatic 29 1-6 2004 105 113
    • (2004) J Mol Catal B Enzymatic , vol.29 , Issue.1-6 , pp. 105-113
    • Cantarella, M.1    Cantarella, L.2    Gallifuoco, A.3    Frezzini, R.4    Spera, A.5    Alfani, F.6
  • 31
    • 0035931535 scopus 로고    scopus 로고
    • Operational stability of Brevibacterium imperialis CBS 489-74 nitrile hydratase
    • F. Alfani, M. Cantarella, A. Spera, and P. Viparelli Operational stability of Brevibacterium imperialis CBS 489-74 nitrile hydratase J Mol Catal B Enzymatic 11 4-6 2001 687 697
    • (2001) J Mol Catal B Enzymatic , vol.11 , Issue.4-6 , pp. 687-697
    • Alfani, F.1    Cantarella, M.2    Spera, A.3    Viparelli, P.4
  • 32
    • 0032431921 scopus 로고    scopus 로고
    • Characterization in UF-membrane reactors of nitrile hydratase from Brevibacterium imperialis CBS 489-74 resting cells
    • M. Cantarella, A. Spera, and F. Alfani Characterization in UF-membrane reactors of nitrile hydratase from Brevibacterium imperialis CBS 489-74 resting cells Ann N Y Acad Sci 864 1998 224 227
    • (1998) Ann N Y Acad Sci , vol.864 , pp. 224-227
    • Cantarella, M.1    Spera, A.2    Alfani, F.3
  • 33
    • 0032475392 scopus 로고    scopus 로고
    • Acrylamide production in an ultrafiltration-membrane bioreactor using cells of Brevibacterium imperialis CBS 489-74
    • M. Cantarella, L. Cantarella, A. Spera, and F. Alfani Acrylamide production in an ultrafiltration-membrane bioreactor using cells of Brevibacterium imperialis CBS 489-74 J Membr Sci 147 1998 279 290
    • (1998) J Membr Sci , vol.147 , pp. 279-290
    • Cantarella, M.1    Cantarella, L.2    Spera, A.3    Alfani, F.4
  • 34
    • 0011352603 scopus 로고
    • Synthesis of acrylamide by Brevibacterium imperialis CBS 489-74 resting cells in UF-membrane reactors
    • ICheaP-2 Scientific Committee, editor.
    • Cantarella M, Spera A, Cesti P, Bianchi, D. Synthesis of acrylamide by Brevibacterium imperialis CBS 489-74 resting cells in UF-membrane reactors. In: ICheaP-2 Scientific Committee, editor. AIDIC Conference Series, vol. 1. 1995. p. 369-77.
    • (1995) AIDIC Conference Series , vol.1 , pp. 369-377
    • Cantarella, M.1    Spera, A.2    Cesti, P.3    Bianchi, D.4
  • 35
    • 27844531561 scopus 로고    scopus 로고
    • Nitrile bioconversion by Microbacterium imperiale CBS 498-74 resting cells in batch and UF-membrane bioreactors
    • M. Cantarella, L. Cantarella, A. Gallifuoco, and A. Spera Nitrile bioconversion by Microbacterium imperiale CBS 498-74 resting cells in batch and UF-membrane bioreactors J Ind Microbiol Biotechnol 2005 (published online 1st March)
    • (2005) J Ind Microbiol Biotechnol
    • Cantarella, M.1    Cantarella, L.2    Gallifuoco, A.3    Spera, A.4
  • 36
    • 2442498482 scopus 로고    scopus 로고
    • A control of the nitrile-hydrolyzing enzyme activity in Rhodococcus rhodochrous IFO 15564; Preferential action of nitrile hydratase and amidase depending on the reaction condition factors and its application to the one-pot preparation of amides from aldehydes
    • M. Kashiwagi, K. Fuhshuku, and T. Sugai A control of the nitrile-hydrolyzing enzyme activity in Rhodococcus rhodochrous IFO 15564; preferential action of nitrile hydratase and amidase depending on the reaction condition factors and its application to the one-pot preparation of amides from aldehydes J Mol Catal B Enzymatic 29 2004 249 258
    • (2004) J Mol Catal B Enzymatic , vol.29 , pp. 249-258
    • Kashiwagi, M.1    Fuhshuku, K.2    Sugai, T.3


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