메뉴 건너뛰기




Volumn 92, Issue 2, 2005, Pages 137-146

Biotransformation of R-2-hydroxy-4-phenylbutyric acid by D lactate dehydrogenase and Candida boidinii cells containing formate dehydrogenase coimmobilized in a fibrous bed bioreactor

Author keywords

Biotransformation; Fibrous bed bioreactor; Formate dehydrogenase; Immobilization; Lactate dehydrogenase; R 2 hydroxy 4 phenylbutyric acid

Indexed keywords

BIOREACTORS; BIOTECHNOLOGY; CELL CULTURE; CONCENTRATION (PROCESS); ENZYME INHIBITION; OXIDATION; REACTION KINETICS;

EID: 27744528589     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20582     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0036010270 scopus 로고    scopus 로고
    • Immobilization of beta-galactosidase on fibrous matrix by polyethyleneimine for production of galacto-oligosaccharides from lactose
    • Albayrak N, Yang ST. 2002. Immobilization of beta-galactosidase on fibrous matrix by polyethyleneimine for production of galacto-oligosaccharides from lactose. Biotechnol Prog 18:240-251.
    • (2002) Biotechnol Prog , vol.18 , pp. 240-251
    • Albayrak, N.1    Yang, S.T.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the detection of microgram quantities of proteins
    • Bradford MA. 1976. A rapid and sensitive method for the detection of microgram quantities of proteins. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.A.1
  • 5
    • 0002938341 scopus 로고    scopus 로고
    • Immobilized enzymes in bioprocess
    • D'Souza SF. 1999. Immobilized enzymes in bioprocess. Curr Sci 77:69-79.
    • (1999) Curr Sci , vol.77 , pp. 69-79
    • D'Souza, S.F.1
  • 6
    • 0026173106 scopus 로고
    • A method for the preparation of coimmobilizates by adhesion using polyethylenimine
    • D'Souza SF, Melo JS. 1991. A method for the preparation of coimmobilizates by adhesion using polyethylenimine. Enzyme Microb Technol 13:508-511.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 508-511
    • D'Souza, S.F.1    Melo, J.S.2
  • 7
    • 0141615071 scopus 로고    scopus 로고
    • Incorporation of alkaline phosphatase into layer-by-layer polyelectrolyte films on the surface of affi-gel heparin beads: Physicochemical characterization and evaluation of the enzyme stability
    • Derbal L, Lesot H, Voegel JC, Ball V. 2003. Incorporation of alkaline phosphatase into layer-by-layer polyelectrolyte films on the surface of affi-gel heparin beads: Physicochemical characterization and evaluation of the enzyme stability. Biomacromolecules 4:1255-1263.
    • (2003) Biomacromolecules , vol.4 , pp. 1255-1263
    • Derbal, L.1    Lesot, H.2    Voegel, J.C.3    Ball, V.4
  • 8
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: Potential and limitations of microbial whole-sell hydrosylations in applied biocatalysis
    • Duetz WA, Beilen JB van, Witholt B. 2001. Using proteins in their natural environment: Potential and limitations of microbial whole-sell hydrosylations in applied biocatalysis. Curr Opin Biotech 12:419-425.
    • (2001) Curr Opin Biotech , vol.12 , pp. 419-425
    • Duetz, W.A.1    Van Beilen, J.B.2    Witholt, B.3
  • 9
    • 0018693848 scopus 로고
    • NAD-dependent formate dehydrogenase from methylotrophic bacterium, strain 1. Purification and characterization
    • Egorov AM, Avilova TV, Dikov MM, Popov VO, Rodionov YV, Berezin IV. 1979. NAD-dependent formate dehydrogenase from methylotrophic bacterium, strain 1. Purification and characterization. Eur J Biochem 99:569-576.
    • (1979) Eur J Biochem , vol.99 , pp. 569-576
    • Egorov, A.M.1    Avilova, T.V.2    Dikov, M.M.3    Popov, V.O.4    Rodionov, Y.V.5    Berezin, I.V.6
  • 10
    • 3042828485 scopus 로고    scopus 로고
    • Enabling multienzyme biocatalysis using nanoporous materials
    • El-Zahab B, Jia H, Wang P. 2004. Enabling multienzyme biocatalysis using nanoporous materials. Biotechnol Bioeng 87:178-183.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 178-183
    • El-Zahab, B.1    Jia, H.2    Wang, P.3
  • 14
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel W, Kula MR. 1989. Dehydrogenases for the synthesis of chiral compounds. Eur J Biochem 184:1-13.
    • (1989) Eur J Biochem , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.R.2
  • 15
    • 37049090023 scopus 로고
    • Synthesis of optically pure R-2-hydroxy acids using D-lactate dehydrogenase
    • Kim MJ, Kim JY. 1991. Synthesis of optically pure R-2-hydroxy acids using D-lactate dehydrogenase. J Chem Soc Chem Commun 5:326-327.
    • (1991) J Chem Soc Chem Commun , vol.5 , pp. 326-327
    • Kim, M.J.1    Kim, J.Y.2
  • 16
    • 10144250281 scopus 로고    scopus 로고
    • Enzyme engineering aspects of biocatalysis: Cofactor regeneration as example
    • Kragl U, Kruse W, Hummel W, Wandrey C. 1996. Enzyme engineering aspects of biocatalysis: Cofactor regeneration as example. Biotechnol Bioeng 52:309-319.
    • (1996) Biotechnol Bioeng , vol.52 , pp. 309-319
    • Kragl, U.1    Kruse, W.2    Hummel, W.3    Wandrey, C.4
  • 18
    • 0032127635 scopus 로고    scopus 로고
    • NAD+/NADH recycling by coimmobilized lactate dehydrogenase and glutamate dehydrogenase
    • Le M, Means GE. 1998. NAD+/NADH recycling by coimmobilized lactate dehydrogenase and glutamate dehydrogenase. Enzyme Microb Technol 23:49-57.
    • (1998) Enzyme Microb Technol , vol.23 , pp. 49-57
    • Le, M.1    Means, G.E.2
  • 19
    • 0034607269 scopus 로고    scopus 로고
    • Reversible enzyme immobilization via a very strong and nondistorting ionic adsorption on support-polyethylenimine composites
    • Mateo C, Abian O, Fernandez-Lafuente R, Guisan JM. 2000. Reversible enzyme immobilization via a very strong and nondistorting ionic adsorption on support-polyethylenimine composites. Biotechnol Bioeng 68:98-105.
    • (2000) Biotechnol Bioeng , vol.68 , pp. 98-105
    • Mateo, C.1    Abian, O.2    Fernandez-Lafuente, R.3    Guisan, J.M.4
  • 20
    • 0038035597 scopus 로고    scopus 로고
    • Poly(ethyleneimine)-immobilized-cloth enzyme immunoassay for the detection of Salmonella lipopolysaccharide
    • Matsumoto K, Sakata M, Iwahashi N, Kunitake M, Miyazaki M, Hirayama C. 2003. Poly(ethyleneimine)-immobilized-cloth enzyme immunoassay for the detection of Salmonella lipopolysaccharide. Immunol Invest 32:3-15.
    • (2003) Immunol Invest , vol.32 , pp. 3-15
    • Matsumoto, K.1    Sakata, M.2    Iwahashi, N.3    Kunitake, M.4    Miyazaki, M.5    Hirayama, C.6
  • 21
    • 4644315650 scopus 로고    scopus 로고
    • Accelerating whole-cell biocatalysis by reducing outer membrance permeability barrier
    • Ni Y, Chen RR. 2004. Accelerating whole-cell biocatalysis by reducing outer membrance permeability barrier. Biotechnol Bioeng 87:804-811.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 804-811
    • Ni, Y.1    Chen, R.R.2
  • 22
    • 0032490702 scopus 로고    scopus 로고
    • Evolution of angiotensin-converting enzyme inhibition in hypertension, heart failure, and vascular protection
    • Parmley WW. 1998. Evolution of angiotensin-converting enzyme inhibition in hypertension, heart failure, and vascular protection. Am J Med 105:27S-31S.
    • (1998) Am J Med , vol.105
    • Parmley, W.W.1
  • 23
    • 0036307726 scopus 로고    scopus 로고
    • Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus
    • Razeto A, Kochhar S, Hottinger H, Dauter M, Wilson KS, Lamzin VS. 2002. Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus. J Mol Biol 318:109-119.
    • (2002) J Mol Biol , vol.318 , pp. 109-119
    • Razeto, A.1    Kochhar, S.2    Hottinger, H.3    Dauter, M.4    Wilson, K.S.5    Lamzin, V.S.6
  • 24
    • 0026625840 scopus 로고
    • Optimization of a process for the production of (R)-2-hydroxy-4- phenylbutyric acid-an intermediate for inhibitors of angiotensin converting enzyme
    • Schmidt E, Ghisalba O, Gygax D, Sedelmeier G. 1992. Optimization of a process for the production of (R)-2-hydroxy-4-phenylbutyric acid-an intermediate for inhibitors of angiotensin converting enzyme. J Biotechnol 24:315-327.
    • (1992) J Biotechnol , vol.24 , pp. 315-327
    • Schmidt, E.1    Ghisalba, O.2    Gygax, D.3    Sedelmeier, G.4
  • 25
    • 0017252385 scopus 로고
    • Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii
    • Schute H, Flossdorf J, Sahm H, Kula MR. 1976. Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. Eur J Biochem 62:151-160.
    • (1976) Eur J Biochem , vol.62 , pp. 151-160
    • Schute, H.1    Flossdorf, J.2    Sahm, H.3    Kula, M.R.4
  • 26
  • 27
    • 0034698380 scopus 로고    scopus 로고
    • Enantio- and chemoselective reduction of 2,4-diketo acid derivatives with cinchona modified Pt-catalyst-synthesis of (R)-2-hydroxy-4-phenylbutyric acid ethyl ester
    • Studer M, Burkhardt S, Indolese AF, Blaser HU. 2000. Enantio- and chemoselective reduction of 2,4-diketo acid derivatives with cinchona modified Pt-catalyst-synthesis of (R)-2-hydroxy-4-phenylbutyric acid ethyl ester. Chem Commun 14:1327-1328.
    • (2000) Chem Commun , vol.14 , pp. 1327-1328
    • Studer, M.1    Burkhardt, S.2    Indolese, A.F.3    Blaser, H.U.4
  • 29
    • 0030199017 scopus 로고    scopus 로고
    • Kinetics and stability of GM-CSF production by recombinant yeast cells immobilized in a fibrous-bed bioreactor
    • Yang ST, Shu CH. 1996. Kinetics and stability of GM-CSF production by recombinant yeast cells immobilized in a fibrous-bed bioreactor. Biotechnol Prog 12:449-456.
    • (1996) Biotechnol Prog , vol.12 , pp. 449-456
    • Yang, S.T.1    Shu, C.H.2
  • 30
    • 16344369425 scopus 로고    scopus 로고
    • Stereospecific synthesis of (R)-2-hydroxy carboxylic acids using recombinant E. coli BL21 overexpressing YiaE from Escherichia coli K12 and glucose dehydrogenase from Bacillus subtilis
    • Yun H, Choi HL, Fadnavis NW, Kim BG. 2005. Stereospecific synthesis of (R)-2-hydroxy carboxylic acids using recombinant E. coli BL21 overexpressing YiaE from Escherichia coli K12 and glucose dehydrogenase from Bacillus subtilis. Biotechnol Prog 21:366-371.
    • (2005) Biotechnol Prog , vol.21 , pp. 366-371
    • Yun, H.1    Choi, H.L.2    Fadnavis, N.W.3    Kim, B.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.