메뉴 건너뛰기




Volumn 23, Issue 2, 2005, Pages 139-153

Effects of internal mass transfer and product inhibition on a simulated immobilized enzyme-catalyzed reactor for lactose hydrolysis

Author keywords

Biocatalysis; Effectiveness factor; Enzyme bioreactors; Immobilisation; Immobilised enzymes; Internal mass transfer; Product inhibition

Indexed keywords

CHEMICAL REACTORS; COMPUTER SIMULATION; ENZYME IMMOBILIZATION; FINITE ELEMENT METHOD; GALERKIN METHODS; HYDROLYSIS; MATHEMATICAL MODELS; REACTION KINETICS;

EID: 13244292422     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2004.10.010     Document Type: Article
Times cited : (40)

References (49)
  • 1
    • 0032524182 scopus 로고    scopus 로고
    • Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromices fragilis
    • Santos, M. Ladero, and F. Garcia-Ochoa Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromices fragilis Enzyme Microb. Technol. 22 1998 558 567
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 558-567
    • Santos1    Ladero, M.2    Garcia-Ochoa, F.3
  • 2
    • 0033527096 scopus 로고    scopus 로고
    • Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-galactosidase
    • I. Petzelbauer, B. Nidetzky, D. Haltrich, and K. Kulbe Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-galactosidase Biotechnol. Bioeng. 64 1999 322 332
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 322-332
    • Petzelbauer, I.1    Nidetzky, B.2    Haltrich, D.3    Kulbe, K.4
  • 3
    • 0029176775 scopus 로고
    • Determination of kinetics parameters for free and immobilized β-galactosidase
    • C.R. Carrara, and A.C. Rubiolo Determination of kinetics parameters for free and immobilized β-galactosidase Process Biochem. 31 1995 243 248
    • (1995) Process Biochem. , vol.31 , pp. 243-248
    • Carrara, C.R.1    Rubiolo, A.C.2
  • 4
    • 0344878873 scopus 로고    scopus 로고
    • A method for evaluating lactose hydrolysis in a fixed bed reactor with β-galactosidase immobilized on chitson
    • C.R. Carrara, and A.C. Rubiolo A method for evaluating lactose hydrolysis in a fixed bed reactor with β-galactosidase immobilized on chitson Chem. Eng. J. 65 1997 93 98
    • (1997) Chem. Eng. J. , vol.65 , pp. 93-98
    • Carrara, C.R.1    Rubiolo, A.C.2
  • 5
    • 0024731296 scopus 로고
    • A new graphical method for determining parameters in Michaelis-Menten- type kinetics for enzymatic lactose hydrolysis
    • S.T. Yang, and M.R. Okos A new graphical method for determining parameters in Michaelis-Menten-type kinetics for enzymatic lactose hydrolysis Biotechnol. Bioeng. 34 1989 763 773
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 763-773
    • Yang, S.T.1    Okos, M.R.2
  • 6
    • 0024640088 scopus 로고
    • Hydrolysis of lactose in skim milk by immobilized β-galactosidase in a spiral flow reactor
    • A.P. Bakken, C.G. Hill, and C.H. Amundson Hydrolysis of lactose in skim milk by immobilized β-galactosidase in a spiral flow reactor Biotechnol. Bioeng. 33 1989 1249 1257
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 1249-1257
    • Bakken, A.P.1    Hill, C.G.2    Amundson, C.H.3
  • 7
    • 0027639561 scopus 로고
    • Studies on modeling and simulation of lactose hydrolysis by free and immobilized β-galactosidace from Aspergillus niger
    • N. Papayannakos, G. Markas, and D. Kekos Studies on modeling and simulation of lactose hydrolysis by free and immobilized β-galactosidace from Aspergillus niger Chem. Eng. J. 52 1993 B1 B12
    • (1993) Chem. Eng. J. , vol.52
    • Papayannakos, N.1    Markas, G.2    Kekos, D.3
  • 8
    • 0028821075 scopus 로고
    • Lactose hydrolysis in aqueous two-phase system by whole cell β-galactosidase of Kluyveromyces marxianus
    • M. Tomaska, M. Stredansky, A. Tomaskova, and E. Sturdik Lactose hydrolysis in aqueous two-phase system by whole cell β-galactosidase of Kluyveromyces marxianus Bioprocess Eng. 12 1995 17 20
    • (1995) Bioprocess Eng. , vol.12 , pp. 17-20
    • Tomaska, M.1    Stredansky, M.2    Tomaskova, A.3    Sturdik, E.4
  • 9
    • 0026918541 scopus 로고
    • Comparison between dispersion and plug-flow models for fixed-bed enzyme reactors
    • R. Lortie, and D. Pelletier Comparison between dispersion and plug-flow models for fixed-bed enzyme reactors AIChE J. 38 1992 1477 1480
    • (1992) AIChE J. , vol.38 , pp. 1477-1480
    • Lortie, R.1    Pelletier, D.2
  • 10
    • 0001592799 scopus 로고
    • Flow dynamics of immobilized enzyme reactors
    • C.B. Ching, and Y.Y. Ho Flow dynamics of immobilized enzyme reactors Appl. Microbiol. Biotechnol. 20 1984 303 309
    • (1984) Appl. Microbiol. Biotechnol. , vol.20 , pp. 303-309
    • Ching, C.B.1    Ho, Y.Y.2
  • 11
    • 85047677688 scopus 로고    scopus 로고
    • Predicting the performance of immobilized enzyme reactors using reversible Michaelis-Menten kinetics
    • I.M. Abu-Reesh Predicting the performance of immobilized enzyme reactors using reversible Michaelis-Menten kinetics Bioprocess Eng. 17 1997 131 137
    • (1997) Bioprocess Eng. , vol.17 , pp. 131-137
    • Abu-Reesh, I.M.1
  • 12
    • 0029379758 scopus 로고
    • Fluidized bed reactors operating with immobilized enzyme systems: Design model and its experimental verification
    • A. Bódalo, E. Gómez, J.L. Gomez, J. Bastida, and M.F. Maximo Fluidized bed reactors operating with immobilized enzyme systems: design model and its experimental verification Enzyme Microb. Technol. 17 1995 915 922
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 915-922
    • Bódalo, A.1    Gómez, E.2    Gomez, J.L.3    Bastida, J.4    Maximo, M.F.5
  • 13
    • 0025387872 scopus 로고
    • Modeling of a fluidized bed bioreactor for immobilized enzyme (part 1)
    • T. Kisser, G.A. Oertzen, and W. Bauer Modeling of a fluidized bed bioreactor for immobilized enzyme (part 1) Chem. Eng. Technol. 13 1990 20 26
    • (1990) Chem. Eng. Technol. , vol.13 , pp. 20-26
    • Kisser, T.1    Oertzen, G.A.2    Bauer, W.3
  • 14
    • 0029111281 scopus 로고
    • Analysis of nonisothermal tubular reactor packed with immobilized enzyme systems
    • M.M. Hassan, M. Atiqullah, S.A. Beg, and M. Chowdhury Analysis of nonisothermal tubular reactor packed with immobilized enzyme systems Biochem. Eng. J. 58 1995 275 283
    • (1995) Biochem. Eng. J. , vol.58 , pp. 275-283
    • Hassan, M.M.1    Atiqullah, M.2    Beg, S.A.3    Chowdhury, M.4
  • 15
    • 0030131390 scopus 로고    scopus 로고
    • Effects of enzyme microcapsule shape on the performance of a nonisothermal packed-bed tubular reactor
    • M.M. Hassan, M. Atiqullah, S.A. Beg, and M.H.M. Chowdhury Effects of enzyme microcapsule shape on the performance of a nonisothermal packed-bed tubular reactor J. Chem. Technol. 66 1996 41 55
    • (1996) J. Chem. Technol. , vol.66 , pp. 41-55
    • Hassan, M.M.1    Atiqullah, M.2    Beg, S.A.3    Chowdhury, M.H.M.4
  • 16
    • 0023440194 scopus 로고
    • Theoretical analysis of a packed-bed biological reactor for various reaction kinetics
    • M.M. Hassan, and S.A. Beg Theoretical analysis of a packed-bed biological reactor for various reaction kinetics Chem. Eng. J. 36 1987 15 27
    • (1987) Chem. Eng. J. , vol.36 , pp. 15-27
    • Hassan, M.M.1    Beg, S.A.2
  • 17
    • 0026354787 scopus 로고
    • Development of reactor model for glucose isomerization catalyzed by whole-cell immobilized glucose isomerase
    • D. Vasic-Racki, N. Pavlovic, S. Cizmek, M. Drazic, and B. Husadzic Development of reactor model for glucose isomerization catalyzed by whole-cell immobilized glucose isomerase Bioprocess Eng. 7 1991 183 187
    • (1991) Bioprocess Eng. , vol.7 , pp. 183-187
    • Vasic-Racki, D.1    Pavlovic, N.2    Cizmek, S.3    Drazic, M.4    Husadzic, B.5
  • 18
    • 0021390930 scopus 로고
    • Effect of external mass transfer in a packed-bed reactor system for a reversible enzyme reaction
    • Y.H. Park, M.H. Han, and H.K. Rhee Effect of external mass transfer in a packed-bed reactor system for a reversible enzyme reaction J. Chem. Technol. Biotechnol. 34B 1984 57 69
    • (1984) J. Chem. Technol. Biotechnol. , vol.34 , pp. 57-69
    • Park, Y.H.1    Han, M.H.2    Rhee, H.K.3
  • 19
    • 84985687360 scopus 로고
    • Backmixing and mass transfer in the design of immobilized-enzyme reactors
    • T. Kobayashi, and M. Moo-Young Backmixing and mass transfer in the design of immobilized-enzyme reactors Biotechnol. Bioeng. 13 1971 893 910
    • (1971) Biotechnol. Bioeng. , vol.13 , pp. 893-910
    • Kobayashi, T.1    Moo-Young, M.2
  • 20
    • 0010479905 scopus 로고
    • Modeling of a fixed bed and a fluidized bed immobilized enzyme reactor
    • C.B. Ching, and K.H. Chu Modeling of a fixed bed and a fluidized bed immobilized enzyme reactor Appl. Microbiol. Biotechnol. 29 1988 316 322
    • (1988) Appl. Microbiol. Biotechnol. , vol.29 , pp. 316-322
    • Ching, C.B.1    Chu, K.H.2
  • 21
    • 0022766595 scopus 로고
    • Heterogeneous one-dimensional model for fixed bed enzyme reactors
    • R. Lortie, and D. Thomas Heterogeneous one-dimensional model for fixed bed enzyme reactors Biotechnol. Bioeng. 1986 1256 1260
    • (1986) Biotechnol. Bioeng. , pp. 1256-1260
    • Lortie, R.1    Thomas, D.2
  • 22
    • 0028452839 scopus 로고
    • Evaluation of the performance of immobilized enzyme reactors with Michaelis-Menten kinetics
    • R. Lortie Evaluation of the performance of immobilized enzyme reactors with Michaelis-Menten kinetics J. Chem. Technol. Biotechnol. 60 1994 189 193
    • (1994) J. Chem. Technol. Biotechnol. , vol.60 , pp. 189-193
    • Lortie, R.1
  • 23
    • 0037447614 scopus 로고    scopus 로고
    • Prediction of the fixed-bed reactor behavior using dispersion and plug-flow models with different kinetics for immobilized enzyme
    • C.R. Carrara, E.J. Mammarela, and A.C. Rubiolo Prediction of the fixed-bed reactor behavior using dispersion and plug-flow models with different kinetics for immobilized enzyme Chem. Eng. J. 92 1-3 2002 123 129
    • (2002) Chem. Eng. J. , vol.92 , Issue.1-3 , pp. 123-129
    • Carrara, C.R.1    Mammarela, E.J.2    Rubiolo, A.C.3
  • 24
    • 13244251982 scopus 로고
    • Enzyme immobilized in a packed-bed reactor: Kinetic parameters and mass transfer effects
    • W.N. Marrazzo, and B.J. McCoy Enzyme immobilized in a packed-bed reactor: kinetic parameters and mass transfer effects Biotechnol. Bioeng. 23 1981 1237 1254
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 1237-1254
    • Marrazzo, W.N.1    McCoy, B.J.2
  • 25
    • 0029676356 scopus 로고    scopus 로고
    • An efficient method for solving two-point boundary value problems with extremely high accuracy
    • F. Shiraishi, and S. Fujiwara An efficient method for solving two-point boundary value problems with extremely high accuracy J. Chem. Eng. Jpn. 29 1996 88 94
    • (1996) J. Chem. Eng. Jpn. , vol.29 , pp. 88-94
    • Shiraishi, F.1    Fujiwara, S.2
  • 26
    • 85024262559 scopus 로고
    • Numerical solution of two-point boundary value problem by combined Taylor series method with a technique for rapidly selecting suitable step sizes
    • F. Shiraishi, T. Hasegawa, and H. Nagasue Numerical solution of two-point boundary value problem by combined Taylor series method with a technique for rapidly selecting suitable step sizes J. Chem. Eng. Jpn. 28 1995 306 315
    • (1995) J. Chem. Eng. Jpn. , vol.28 , pp. 306-315
    • Shiraishi, F.1    Hasegawa, T.2    Nagasue, H.3
  • 27
    • 0030168501 scopus 로고    scopus 로고
    • Characteristic of apparent kinetics parameters in a packed-bed immobilized enzyme reactor
    • F. Shiraishi, T. Hasegawa, S. Kasai, N. Makishita, and H. Miyakawa Characteristic of apparent kinetics parameters in a packed-bed immobilized enzyme reactor Chem. Eng. Sci. 51 1996 2847 2852
    • (1996) Chem. Eng. Sci. , vol.51 , pp. 2847-2852
    • Shiraishi, F.1    Hasegawa, T.2    Kasai, S.3    Makishita, N.4    Miyakawa, H.5
  • 28
    • 0029666544 scopus 로고    scopus 로고
    • A computational method for determination of the mass transfer coefficient in packed-bed immobilized enzyme reactors
    • F. Shiraishi, H. Miyakawa, T. Hasegawa, and S. Kasai A computational method for determination of the mass transfer coefficient in packed-bed immobilized enzyme reactors J. Chem. Technol. 66 1996 405 413
    • (1996) J. Chem. Technol. , vol.66 , pp. 405-413
    • Shiraishi, F.1    Miyakawa, H.2    Hasegawa, T.3    Kasai, S.4
  • 29
    • 0032935991 scopus 로고    scopus 로고
    • A highly accurate numerical method for calculating apparent kinetics parameters of immobilized enzyme reactions: 1. Theory
    • H. Miyakawa, H. Nagasue, and F. Shiraishi A highly accurate numerical method for calculating apparent kinetics parameters of immobilized enzyme reactions: 1. Theory Biochem. Eng. J. 3 1999 91 101
    • (1999) Biochem. Eng. J. , vol.3 , pp. 91-101
    • Miyakawa, H.1    Nagasue, H.2    Shiraishi, F.3
  • 30
    • 0032912433 scopus 로고    scopus 로고
    • A highly accurate numerical method for calculating apparent kinetics parameters of immobilized enzyme reactions: 2. Accuracies of calculated values
    • H. Miyakawa, H. Nagasue, and F. Shiraishi A highly accurate numerical method for calculating apparent kinetics parameters of immobilized enzyme reactions: 2. accuracies of calculated values Biochem. Eng. J. 3 1999 103 111
    • (1999) Biochem. Eng. J. , vol.3 , pp. 103-111
    • Miyakawa, H.1    Nagasue, H.2    Shiraishi, F.3
  • 31
    • 0022743071 scopus 로고
    • Analysis of diffusion effects of immobilized enzymes on porous supports with reversible Michaelis-Menten kinetics
    • A. Bódalo, J.L. Gomez, E. Gómez, J. Bastida, J.L. Iborra, and A. Manjon Analysis of diffusion effects of immobilized enzymes on porous supports with reversible Michaelis-Menten kinetics Enzyme Microb. Technol. 8 1986 433 438
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 433-438
    • Bódalo, A.1    Gomez, J.L.2    Gómez, E.3    Bastida, J.4    Iborra, J.L.5    Manjon, A.6
  • 33
    • 0020154406 scopus 로고
    • Modeling enzyme immobilization in porous solid supports
    • D.D. Do, D.S. Clark, and J.E. Bailey Modeling enzyme immobilization in porous solid supports Biotechnol. Bioeng. 24 1982 1527
    • (1982) Biotechnol. Bioeng. , vol.24 , pp. 1527
    • Do, D.D.1    Clark, D.S.2    Bailey, J.E.3
  • 34
    • 0020737182 scopus 로고
    • Structure-function relationships in immobilized chymotrypsin catalysis
    • D.S. Clark, and J.E. Bailey Structure-function relationships in immobilized chymotrypsin catalysis Biotechnol. Bioeng. 25 1983 1027
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 1027
    • Clark, D.S.1    Bailey, J.E.2
  • 35
    • 0021491327 scopus 로고
    • Deactivation kinetics of immobilized α-chymotrypsin subpopulations
    • D.S. Clark, and J.E. Bailey Deactivation kinetics of immobilized α-chymotrypsin subpopulations Biotechnol. Bioeng. 26 1984 1090
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 1090
    • Clark, D.S.1    Bailey, J.E.2
  • 36
    • 0022011829 scopus 로고
    • A mathematical model for restricted diffusion effects on macromolecule impregnation in porous supports
    • D.S. Clark, J.E. Bailey, and D.D. Do A mathematical model for restricted diffusion effects on macromolecule impregnation in porous supports Biotechnol. Bioeng. 27 1985 208
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 208
    • Clark, D.S.1    Bailey, J.E.2    Do, D.D.3
  • 37
    • 0016533486 scopus 로고
    • Mass transfer and biochemical reaction in enzyme membrane reactor system 2 expanded analysis for single enzyme system
    • R. Shyan, B. Davidsson, and W.R. Vieth Mass transfer and biochemical reaction in enzyme membrane reactor system 2 expanded analysis for single enzyme system Chem. Eng. Sci. 30 1975 669 678
    • (1975) Chem. Eng. Sci. , vol.30 , pp. 669-678
    • Shyan, R.1    Davidsson, B.2    Vieth, W.R.3
  • 38
    • 0018435112 scopus 로고
    • The effects of mass transfer resistances on encapsulated enzymatic reaction systems
    • S.H. Lin The effects of mass transfer resistances on encapsulated enzymatic reaction systems Chem. Eng. J. 17 1979 55 61
    • (1979) Chem. Eng. J. , vol.17 , pp. 55-61
    • Lin, S.H.1
  • 39
    • 0023421237 scopus 로고
    • Evaluation of effectiveness factor along immobilized enzyme fixed-bed reactors: Design of a reactor with naringinase covalently immobilized into glycophase coated porous class
    • A. Manjon, J.L. Iborra, J.L. Gomez, E. Gómez, J. Bastida, and A. Bódalo Evaluation of effectiveness factor along immobilized enzyme fixed-bed reactors: design of a reactor with naringinase covalently immobilized into glycophase coated porous class Biotechnol. Bioeng. 30 1987 491 497
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 491-497
    • Manjon, A.1    Iborra, J.L.2    Gomez, J.L.3    Gómez, E.4    Bastida, J.5    Bódalo, A.6
  • 40
    • 0035811851 scopus 로고    scopus 로고
    • Mass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of Racemate in a fixed-bed reactor
    • G.-H. Xiu, L. Jiang, and Li Ping Mass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of Racemate in a fixed-bed reactor Biotechnol. Bioeng. 74 2001 29 39
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 29-39
    • Xiu, G.-H.1    Jiang, L.2    Li, P.3
  • 41
    • 24444437044 scopus 로고
    • Continuous flow systems, distribution of residence times
    • P.V. Danckwerts Continuous flow systems, distribution of residence times Chem. Eng. Sci. 2 1953 1 18
    • (1953) Chem. Eng. Sci. , vol.2 , pp. 1-18
    • Danckwerts, P.V.1
  • 44
    • 0032477383 scopus 로고    scopus 로고
    • A technique for accurate collocation residual calculations
    • R.A. Adomaitis, and Y.-H. Lin A technique for accurate collocation residual calculations Chem. Eng. J. 71 1998 127 134
    • (1998) Chem. Eng. J. , vol.71 , pp. 127-134
    • Adomaitis, R.A.1    Lin, Y.-H.2
  • 46
    • 0032477383 scopus 로고    scopus 로고
    • A technique for accurate collocation residual calculations
    • R.A. Adomaitis, and Y.-H. Lin A technique for accurate collocation residual calculations Chem. Eng. J. 71 1998 127 134
    • (1998) Chem. Eng. J. , vol.71 , pp. 127-134
    • Adomaitis, R.A.1    Lin, Y.-H.2
  • 47
    • 0033179967 scopus 로고    scopus 로고
    • MWRtools: A library for weighted residual method calculations
    • Yi-hung Lin, H.-Y. Chang, and R.A. Adomaitis MWRtools: a library for weighted residual method calculations Comput. Chem. Eng. 23 1999 1041 1061
    • (1999) Comput. Chem. Eng. , vol.23 , pp. 1041-1061
    • Yi-Hung, L.1    Chang, H.-Y.2    Adomaitis, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.