메뉴 건너뛰기




Volumn 21, Issue 6, 2003, Pages 349-356

Co-immobilization of D-hydantoinase and D-carboamylase on chitin: Application to the synthesis of p-hydroxyphenylglycine

Author keywords

Agrobacterium radiobacter; Chitin; Co immobilization; D hydantoinase; N carbamyl D amino acid amidohydrolase

Indexed keywords

ADSORPTION; AMINO ACIDS; BACTERIA; BIOSYNTHESIS; CHITIN; COBALT; DERIVATIVES; PH EFFECTS;

EID: 0442310659     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.1080/10242420310001597829     Document Type: Article
Times cited : (22)

References (32)
  • 1
    • 0442293252 scopus 로고    scopus 로고
    • The immobilization of tyrosinase on chitin and chitosan and its possible use in wastewater treatment
    • (Eds. Peter, M.G., Domard A. and Muzzarelli R.) Universität Postdam, Postdam
    • Acosta, N., Cid, C., Aranaz, I. and Heras, A. (2000) "The immobilization of tyrosinase on chitin and chitosan and its possible use in wastewater treatment", In: Advances in Chitin Science 4. (Eds. Peter, M.G., Domard A. and Muzzarelli R.) Universität Postdam, Postdam, pp 159-164.
    • (2000) Advances in Chitin Science , vol.4 , pp. 159-164
    • Acosta, N.1    Cid, C.2    Aranaz, I.3    Heras, A.4
  • 2
    • 0032530505 scopus 로고    scopus 로고
    • Biocatalysis to amino acid -based chiral pharmaceuticals examples and perspectives
    • Brommarius, A.S., Schwarm, M. and Drauz, K. (1998) Biocatalysis to amino acid -based chiral pharmaceuticals examples and perspectives", J. Mol Catal B-Enzym 5, 1-11.
    • (1998) J. Mol Catal B-Enzym , vol.5 , pp. 1-11
    • Brommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 3
    • 0004258374 scopus 로고
    • In: Patai, S., ed; (John Wiley and Sons, London, UK)
    • Capozzi, G. and Modena, G. (1974) In: Patai, S., ed, The Chemistry of the Thiol Groups (John Wiley and Sons, London, UK.), pp 785-857.
    • (1974) The Chemistry of the Thiol Groups , pp. 785-857
    • Capozzi, G.1    Modena, G.2
  • 4
    • 4243463606 scopus 로고
    • Immobilized cell technology in food processing
    • In: Wijffels, R., Buitelaar, R.M., Bucke C. and Tramper, J., eds; (Elsevier, Amsterdam)
    • Champagne, C.P. (1994) "Immobilized cell technology in food processing", In: Wijffels, R., Buitelaar, R.M., Bucke C. and Tramper, J., eds, Immobilized Cells: Basics and Applications (Elsevier, Amsterdam), pp 633-640.
    • (1994) Immobilized Cells: Basics and Applications , pp. 633-640
    • Champagne, C.P.1
  • 5
    • 0036402008 scopus 로고    scopus 로고
    • Enhancing oxidative resistance of Agrobacterium radiobacter N-carbamoyl d-aminoacid amidohydrolase by engineering solvent-accesible methionine residues
    • Chien, H.-C.R., Hsu, C.L., Hu, H.-Y., Wang, W.C. and Hsu, W.-H. (2002) "Enhancing oxidative resistance of Agrobacterium radiobacter N-carbamoyl d-aminoacid amidohydrolase by engineering solvent-accesible methionine residues", Biochem. Bioph. Res. Co. 297, 282-287.
    • (2002) Biochem. Bioph. Res. Co. , vol.297 , pp. 282-287
    • Chien, H.-C.R.1    Hsu, C.L.2    Hu, H.-Y.3    Wang, W.C.4    Hsu, W.-H.5
  • 6
    • 0028971667 scopus 로고
    • Properties of D-hydantoinase from Agrobacterium tumefaciens and its use for the preparation of N-carbamyl D-amino acids
    • Durham, D.-R. and Weber, J.-E. (1995) "Properties of D-hydantoinase from Agrobacterium tumefaciens and its use for the preparation of N-carbamyl D-amino acids", Biochem. Bioph. Res. Co. 216, 1095-1100.
    • (1995) Biochem. Bioph. Res. Co. , vol.216 , pp. 1095-1100
    • Durham, D.-R.1    Weber, J.-E.2
  • 7
    • 0034904521 scopus 로고    scopus 로고
    • Purification of D-hydantoinase from adzuki bean and its immobilization for N-carbamoyl-D-phenylglycine production
    • Fan, C.H. and Lee, C.K. (2001) "Purification of D-hydantoinase from adzuki bean and its immobilization for N-carbamoyl-D-phenylglycine production", Biochem. Eng. J. 8, 157-164.
    • (2001) Biochem. Eng. J. , vol.8 , pp. 157-164
    • Fan, C.H.1    Lee, C.K.2
  • 8
    • 0030140441 scopus 로고    scopus 로고
    • The immobilized porcine pancreatic exopeptidases and its application in casein hydrolysates debittering
    • Ge, S.J. and Zhang, L.-X. (1996) "The immobilized porcine pancreatic exopeptidases and its application in casein hydrolysates debittering", Appl. Biochem. Biotech. 59, 159-165.
    • (1996) Appl. Biochem. Biotech. , vol.59 , pp. 159-165
    • Ge, S.J.1    Zhang, L.-X.2
  • 10
    • 0029887662 scopus 로고    scopus 로고
    • Topological mapping of the cysteine residues of N-carbamyl-Damino acid amidohydrolase and their role in enzymatic activity
    • Grifantini, R., Preseti, C., Galli, G. and Grandi, G. (1996) "Topological mapping of the cysteine residues of N-carbamyl-Damino acid amidohydrolase and their role in enzymatic activity", J. Biol. Chem. 16, 9326-9331.
    • (1996) J. Biol. Chem. , vol.16 , pp. 9326-9331
    • Grifantini, R.1    Preseti, C.2    Galli, G.3    Grandi, G.4
  • 11
    • 84911224702 scopus 로고
    • Influence of the solvent and the solid support on the microenvironment of immobilized alpha-chymotripsin
    • In: Tramper, J., ed; (Elsevier, Amsterdam)
    • Heras, A., Martin, M.T., Acosta, N. and Debaillon-Vesque, F. (1992) "Influence of the solvent and the solid support on the microenvironment of immobilized alpha-chymotripsin", In: Tramper, J., ed, Biocatalysis in Non-conventional Media (Elsevier, Amsterdam), pp 339-346.
    • (1992) Biocatalysis in Non-Conventional Media , pp. 339-346
    • Heras, A.1    Martin, M.T.2    Acosta, N.3    Debaillon-Vesque, F.4
  • 12
    • 0343288985 scopus 로고    scopus 로고
    • N-methylene phosphonic chitosan: A novel soluble derivative
    • Heras, H., Rodríguez, A., Ramos, V. and Agulló, E. (2001) "N-methylene phosphonic chitosan: A novel soluble derivative", Carbohyd. Polym. 44(1), 1-8.
    • (2001) Carbohyd. Polym. , vol.44 , Issue.1 , pp. 1-8
    • Heras, H.1    Rodríguez, A.2    Ramos, V.3    Agulló, E.4
  • 13
    • 77957066180 scopus 로고    scopus 로고
    • Screening of immobilization materials for anaerobic wastewater treatment
    • In: Wijffels, R., Buitelaar, R.M., Bucke, C. and Tramper, J., eds; (Elsevier, Amsterdam)
    • Hwu, C.S. and Tseng, S.K. (1996) "Screening of immobilization materials for anaerobic wastewater treatment", In: Wijffels, R., Buitelaar, R.M., Bucke, C. and Tramper, J., eds, Immobilized Cells: Basics and Applications (Elsevier, Amsterdam), pp 98-105.
    • (1996) Immobilized Cells: Basics and Applications , pp. 98-105
    • Hwu, C.S.1    Tseng, S.K.2
  • 14
    • 0035931579 scopus 로고    scopus 로고
    • Effect of modulation of enzyme inactivation on temperature optimization for reactor operation with chitin-immobilized lactase
    • Illanes, A., Wilson, L. and Tomasello, G. (2001) "Effect of modulation of enzyme inactivation on temperature optimization for reactor operation with chitin-immobilized lactase", J. Mol. Catal. B-Enzym. 11, 531-540.
    • (2001) J. Mol. Catal. B-Enzym. , vol.11 , pp. 531-540
    • Illanes, A.1    Wilson, L.2    Tomasello, G.3
  • 15
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butil hydroperoxide as a probe for methionine oxidation in proteins
    • Keck, R.G. (1996) "The use of t-butil hydroperoxide as a probe for methionine oxidation in proteins", Anal. Biochem. 236, 52-62.
    • (1996) Anal. Biochem. , vol.236 , pp. 52-62
    • Keck, R.G.1
  • 16
    • 0028014309 scopus 로고
    • Enhancement of operational stability of immobilized whole cell D-hydantoinase
    • Kim, D.G., Kim, G.J. and Kim, H.S. (1994) "Enhancement of operational stability of immobilized whole cell D-hydantoinase", Biotechnol. Lett. 16(1), 11-16.
    • (1994) Biotechnol. Lett. , vol.16 , Issue.1 , pp. 11-16
    • Kim, D.G.1    Kim, G.J.2    Kim, H.S.3
  • 17
    • 0034938628 scopus 로고    scopus 로고
    • Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins
    • Kim, Y.H., Berry, A.H., Spencer, D.A. and Sittes, W.E. (2001). "Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins", Protein Eng. 14(5), 343-347.
    • (2001) Protein Eng. , vol.14 , Issue.5 , pp. 343-347
    • Kim, Y.H.1    Berry, A.H.2    Spencer, D.A.3    Sittes, W.E.4
  • 18
    • 0345200377 scopus 로고    scopus 로고
    • Development of mercury biotransformation process in fluidized bed reactor with immobilized microorganisms
    • In: Wijffels, R., Buitelaar, R.M., Bucke, C. and Tramper, J., eds; (Elsevier, Amsterdam)
    • Ledakowicz, S., Becker, U. and Deckwer, W.D. (1996). "Development of mercury biotransformation process in fluidized bed reactor with immobilized microorganisms", In: Wijffels, R., Buitelaar, R.M., Bucke, C. and Tramper, J., eds, Immobilized Cells: Basics and Applications (Elsevier, Amsterdam), pp 800-807.
    • (1996) Immobilized Cells: Basics and Applications , pp. 800-807
    • Ledakowicz, S.1    Becker, U.2    Deckwer, W.D.3
  • 19
    • 84978701453 scopus 로고    scopus 로고
    • Amino acids technical production and use
    • In: Rehm, H.-J., Reed, G., Pühler, A. and Stadler, P., eds; (VCH-Verlag, Weinheim)
    • Leuchtenber, W. (1996). "Amino acids technical production and use", In: Rehm, H.-J., Reed, G., Pühler, A. and Stadler, P., eds, Biotechnology (VCH-Verlag, Weinheim), pp 465-502.
    • (1996) Biotechnology , pp. 465-502
    • Leuchtenber, W.1
  • 20
    • 0030446221 scopus 로고    scopus 로고
    • The purification and characterization of a novel D(-)specific carbamoylase enzyme from an Agrobacterium sp
    • Louwrier, A. and Knowles, C.J. (1996). "The purification and characterization of a novel D(-)specific carbamoylase enzyme from an Agrobacterium sp", Enzyme Microb. Tech. 19, 562-571.
    • (1996) Enzyme Microb. Tech. , vol.19 , pp. 562-571
    • Louwrier, A.1    Knowles, C.J.2
  • 21
    • 0442308884 scopus 로고    scopus 로고
    • Co-immobilization of enzymes and cells on chitin and derivatives
    • In: Ballesteros, A., Plou, F.-J., Iborra, J. and Halling, P.-J., eds; (Elsevier, Amsterdam)
    • Martin, A.-B., Picciolato, M. and Heras, A. (1998). "Co-immobilization of enzymes and cells on chitin and derivatives", In: Ballesteros, A., Plou, F.-J., Iborra, J. and Halling, P.-J., eds, Progress in Biotechnology: Stability and Stabilization of Biocatalysts, Vol. 15 (Elsevier, Amsterdam), pp 679-684.
    • (1998) Progress in Biotechnology: Stability and Stabilization of Biocatalysts , vol.15 , pp. 679-684
    • Martin, A.-B.1    Picciolato, M.2    Heras, A.3
  • 22
    • 0024094367 scopus 로고
    • Stereo and substrate-specificity of a D-hydantoinase and a D-acid amidohydrolase of Arthrobacter crystallopoietes AM 2
    • Moller, A., Syldatk, C., Schulze, M. and Wagner, F. (1988). "Stereo and substrate-specificity of a D-hydantoinase and a D-acid amidohydrolase of Arthrobacter crystallopoietes AM 2", Enzyme Microb. Tech. 10(10), 618-625.
    • (1988) Enzyme Microb. Tech. , vol.10 , Issue.10 , pp. 618-625
    • Moller, A.1    Syldatk, C.2    Schulze, M.3    Wagner, F.4
  • 24
    • 0000995575 scopus 로고
    • Enzymatic conversion of N-carbamoyl-D-amino acids to amino acids
    • Olivieri, R., Fascetti, E., Angelini, L. and Degen, I. (1979). "Enzymatic conversion of N-carbamoyl-D-amino acids to amino acids", Enzyme Microb. Tech. 1, 201-204.
    • (1979) Enzyme Microb. Tech. , vol.1 , pp. 201-204
    • Olivieri, R.1    Fascetti, E.2    Angelini, L.3    Degen, I.4
  • 25
    • 0019781513 scopus 로고
    • Microbial transformation of racemic hydantoins to D-amino acids
    • Olivieri, R., Fascetti, E., Angelini, L. and Degen, I. (1981). "Microbial transformation of racemic hydantoins to D-amino acids", Biotechnol. Bioeng. 23, 2173-2183.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 2173-2183
    • Olivieri, R.1    Fascetti, E.2    Angelini, L.3    Degen, I.4
  • 26
    • 0025010775 scopus 로고
    • Properties of the hydantoinase from Agrobacterium sp. IP I-671
    • Runser, S. and Ohleyer, E. (1990). "Properties of the hydantoinase from Agrobacterium sp. IP I-671", Biotechnol. Lett. 12, 259-264.
    • (1990) Biotechnol. Lett. , vol.12 , pp. 259-264
    • Runser, S.1    Ohleyer, E.2
  • 28
    • 0002548361 scopus 로고
    • Microbial and enzymatic production of L-amino acids from D,L-5 monosubstituted hydantoins
    • In: Rozell, D. and Wagner, F., eds; (Hanser Publishers, München)
    • Syldatk, C., Müller, M., Pietzsch, M. and Wagner, F. (1992). "Microbial and enzymatic production of L-amino acids from D,L-5 monosubstituted hydantoins", In: Rozell, D. and Wagner, F., eds, Biocatalytic Production of Amino Acids and Derivatives (Hanser Publishers, München), pp 129-176.
    • (1992) Biocatalytic Production of Amino Acids and Derivatives , pp. 129-176
    • Syldatk, C.1    Müller, M.2    Pietzsch, M.3    Wagner, F.4
  • 29
    • 0001150165 scopus 로고
    • Microbial transformation of hydantoins to N-carbamyl-D-amino acids
    • Takashi, S., Ohashi, T., Kii, Y., Kumaga, H. and Yamada, H. (1979). "Microbial transformation of hydantoins to N-carbamyl-D-amino acids", J. Ferment. Technol. 4, 328-332.
    • (1979) J. Ferment. Technol. , vol.4 , pp. 328-332
    • Takashi, S.1    Ohashi, T.2    Kii, Y.3    Kumaga, H.4    Yamada, H.5
  • 30
    • 0037070481 scopus 로고    scopus 로고
    • A novel method for the immobilization of glucoamylase to produce glucose from maltodextrin
    • Tanriseven, A., Uludag, B.Y. and Dogan, S. (2002). "A novel method for the immobilization of glucoamylase to produce glucose from maltodextrin", Enzyme Microb. Tech. 30, 406-409.
    • (2002) Enzyme Microb. Tech. , vol.30 , pp. 406-409
    • Tanriseven, A.1    Uludag, B.Y.2    Dogan, S.3
  • 32
    • 0035895433 scopus 로고    scopus 로고
    • Crystal structure and site-directed mutagenesis studies on N-Carbamoyl-D-Amino-Acid Amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft
    • Wang, W.C., Hsu, W.-H., Chien, F.T. and Chen, C.Y. (2001). "Crystal structure and site-directed mutagenesis studies on N-Carbamoyl-D-Amino-Acid Amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft", J. Mol. Biol. 306, 251-261.
    • (2001) J. Mol. Biol. , vol.306 , pp. 251-261
    • Wang, W.C.1    Hsu, W.-H.2    Chien, F.T.3    Chen, C.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.