Enzyme Deactivation in Reactors

References

• Bachler M H., Strandberg G. W., Smiley K. L. Starch Conversion By Immobilized Glucoamylase. Biotechnol. Bioeng. 1970; 12: 85–92
   Google Scholar
• Bernfeld P., Bieber R. E., Watson D. M. Kinetics Of Water-Insoluble Phosphoglycerate Mutase. Biochim. Biophys. Acta 1969; 191: 570–78
   Google Scholar
• Butt J. B., Watcher C. K., Billimora R. M. On the Separability Of Catalytic Deactivation Kinetics. Chem. Eng. Sci. 1978; 33: 1321–29
   Web of Science ®Google Scholar
• Buchholz K., Godelman B. Macrokinetics and Operational Stability Of Immobilized Glucose Oxidase and Catalase. Biotechnol. Bioeng. 1978; 20: 1201–20
   Google Scholar
• Chen K C., Chang C. M. Operational Stability Of Immobilized D-Glucose Isomerase In A Continuous Feed Stirred Tank Reactor. Enz. Microb. Technol. 1984; 6: 359–64
   Google Scholar
• Chibata I., Tosa T., Sato T., Mori T. Immobilized Enzymes, Chapter 1, Introduction, I. Chibata. J. Wiley and Sons, New York
   Google Scholar
• Chou A., Ray W. H., Aris R. Simple Control Policies For Reactors With Catalyst Decay. Trans. Inst. Chem. Engrs. 1967; 45: T153–59
   Google Scholar
• Crowe C. M. Optimization Of Reactors With Catalyst Decay I. Single Tubular Reactor With Uniform Temperature. Can. J. Chem. Eng. 1970; 48: 576–84
   Web of Science ®Google Scholar
• Crowe C. M., Lee S. I. Optimization Of Reactors With Catalyst Decay III. Tubular Reactor With Several Beds Of Uniform Temperature. Can. J. Chem. Eng. 1971; 49: 385–90
   Web of Science ®Google Scholar
• Crowe C. M., Therien N. Optimization By Distributed Control Of Reactors With Decaying Catalyst Part 1. Non-Linear Catalyst Deactivation. Can. J. Chem. Eng. 1974; 52: 810–21
   Google Scholar
• Datta R., Armiger W., Ollis D. F. Lysis Of Micrococcus Lysodeikticus by Lysozyme Covalently Immobilized On Cellulose And Polyacrylamide. Biotechnol. Bioeng. 1973; 15: 993–1006
   Web of Science ®Google Scholar
• Goldman R., Kedem O., Silman I. H., Caplan S. R., Katchalski E. Papain-Colloidion Membranes. I. Preparation And Properties. Biochemistry 1968; 7: 486–500
   PubMedGoogle Scholar
• Goldstein L., Levin Y., Pecht M., Katchalski E. Water-Insoluble Enzymes. Synthesis Of A New Carrier And Its Utilization For Preparation Of Insoluble Derivatives of Papain, Trypsin, and Subtilopeptidase. Israel J. Chem. 1967; 5: 90–7
   Google Scholar
• Goldstein L., Levin Y., Katchalski E. A Water-Insoluble Polyanionic Derivative Of Trypsin. II. Effect Of The Polyelectrolyte Carrier On The Kinetic Behavior Of The Bound Trypsin. Biochemistry 1964; 3: 1913–19
   PubMed Web of Science ®Google Scholar
• Gondo S., Sato T., Kusunoki K. Note On The Lineweaver-Burk Plots For The Insolubilized Enzyme Particle. Chem. Eng. Sci. 1973; 28: 1773
   Google Scholar
• Haas W. R., Tavlarides L. L., Wnek W. J. Optimal Temperature Policy For Reversible Reactions With Deactivation: Applied To Enzyme Reactors. AlChE J. 1974; 20: 707–12
   Google Scholar
• Haldane J. B. S. Enzymes. Longmans Green, London 1930; 64
   Google Scholar
• Havewala N. B., Pitcher W. H., Jr. Immobilized Glucose Isomerase For The Production Of High Fructose Syrups. Enzyme Engineering, E. K. Pye, L. B. Wingard, Jr. Plenum Press, New York 1974; Vol. 2: 315–24
   Google Scholar
• Henley J. P., Sadana A. On The Influence Of Severe Internal Diffusional Limitations On Optimum Temperature Operations Criterion And Policies In Deactivating Fixed-Bed And Batch Reactors. Chem. Eng. Commun. 1986; 49: 291–8
   Google Scholar
• Korus R. A., O'Driscoll K. F. The Influence Of Diffusion On The Apparent Rate Of Denaturation Of Gel Entrapped Enzymes. Biotechnol. Bioeng. 1975; 17: 441–44
   Google Scholar
• Krishnaswamy S., Kittrell J. R. Effect Of External Diffusion On Deactivation Rates. AlChE J. 1981; 27: 125–31
   Web of Science ®Google Scholar
• Laidler K. J., Bunting P. S. The Chemical Kinetics Of Enzyme Action2nd ed. Clarendon Press, Oxford 1973; 117
   Google Scholar
• Lamba H. S., Dudukovic M. P. Chemical Reaction Engineering-II, H. M. Hulburt. ACS. 1974; Vol. 133: 106
   Google Scholar
• Lee S. I., Crowe C. M. On Temperature Policies For Batch Reactors With Decaying Catalyst. Chem. Eng. Sci. 1970a; 25: 743–4
   Web of Science ®Google Scholar
• Lee S. I., Crowe C. M. The Optimization Of Reactors With Decaying Catalyst: The Effect Of Macromixing. Can. J. Chem. Eng. 1970b; 48: 192–5
   Web of Science ®Google Scholar
• Lee D. D., Lee Y. Y., Reilly P. J., Collins E. V., Jr., Tsao G. T. Pilot Plant Production Of Glucose With Glucoamylase Immobilized To Porous Silica. Biotechnol. Bioeng. 1976a; 18: 253–67
   Google Scholar
• Lee Y. Y., Fratzke A. A., Wun K., Tsao G. T. Glucose Isomerase Immobilized On Porous Glass. Biotechnol. Bioeng. 1976b; 18: 389–413
   Web of Science ®Google Scholar
• Lee Y. Y., Wun K., Tsao G. T. Kinetics And Mass Transfer Characteristics Of Glucose Isomerase On Porous Glass. Paper 11a., AIChE Meeting. Pittsburgh 1974
   Google Scholar
• Levenspiel O. Chemical Reactor Omnibook. Oregon State University Press, Corvallis 1979
   Google Scholar
• Levenspiel O., Sadana A. The Optimum Temperature Policy For A Deactivating Catalytic Packed Bed Reactive. Chem. Eng. Sci. 1978; 33: 1393–4
   Web of Science ®Google Scholar
• Levin Y., Pecht M., Goldstein L., Katchalski E. A Water Insoluble Polyanionic Derivative Of Trypsin. I. Preparation And Properties. Biochemistry 1964; 3: 1905–13
   PubMed Web of Science ®Google Scholar
• Marconi W., Gulinelli S., Morisi F. Insolubilized Enzymes, M. Salmona, C. Saronio, et al. Raven, New York 1974
   Google Scholar
• Murray M. A., John V. T. Generalized Optimal Flow Rate Policy For Continuous Stirred Tank Reactors With Deactivating Catalysts. Reprint, AIChE Meeting. Boston August, 1986; 25–28
   Google Scholar
• Ogunye A. F., Ray W. H. Non-Simple Control Policies For Reactors With Catalyst Decay. Trans. Inst. Chem. Engrs. 1968; T225–31
   Google Scholar
• Ollis D. F. Diffusional Influences In Denaturable Insolubilized Enzyme Catalysts. Biotechnol. Bioeng. 1972; 15: 871–84
   Google Scholar
• Ollis D. F., Datta R. Optimization Of Activities Of Immobilized Lysozyme, α-chymotrypsin, and Lipase. 25th Southeastern Regional Meeting. ACS, Charleston, SC November, 1973; 7–9
   Google Scholar
• O'Neill S. P. Inactivation Of Immobilized Catalase By Hydrogen Peroxide In Continuous Reactors. Biotechnol. Bioeng. 1972a; 14: 201–05
   Web of Science ®Google Scholar
• O'Neill S. P. Thermal Inactivation Of Immobilized Enzymes In Ideal Continuous Reactors. Biotechnol. Bioeng. 1972b; 14: 473–91
   Google Scholar
• Ooshima H., Hirano Y. Effects Of Mass-Transfer Resistance On Apparent Stability And Performance Of Fixed-Bed Immobilized Enzyme Reactors: Theory And Experiments With Immobilized Invertase. Biotechnol. Bioeng. 1983; 25: 143–55
   Google Scholar
• Park J. Y., Levenspiel O. Optimum Operating Cycle For Systems With Deactivating Catalysts. 2. Applications To Reactors. Ind. Eng. Chem. Process. Design Develop. 1976; 15: 538–544
   Web of Science ®Google Scholar
• Patwardhan V. S., Sadana A. The Optimum Temperature Policy For A Deactivating Immobilized Enzyme Fixed-Bed Reactor. Chem. Eng. Commun. 1982; 15: 169–77
   Web of Science ®Google Scholar
• Pitcher W. H., Jr. Engineering Of Immobilized Enzyme Systems. Catal. Rev. Sci. Eng. 1975; 12: 37–102
   Web of Science ®Google Scholar
• Pontryagin L. S., Boltyanskii V. G., Gamkrelidze R. V., Mishchenko E. F. The Mathematical Theory Of Optimal Processes, K. C. Trircgoff. Interscience Publishers, Inc, New York 1962
   Google Scholar
• Ramachandaran K. B., Perlmutter D. D. Effects Of Immobilization On The Kinetics Of Enzyme-Catalyzed Reactions. I. Glucose Oxidase In A Recirculation Reactor System. Biotechnol. Bioeng. 1976a; 18: 669–84
   Google Scholar
• Ramachandaran K. B., Perlmutter D. D. Effects Of Immobilization On The Kinetics Of Enzyme-Catalyzed Reactions. II. Urease In A Packed-Column Differential Reactor System. Biotechnol. Bioeng. 1976b; 18: 685–99
   Google Scholar
• Reuss M., Buchholz K. Analysis Of The Coupled Transport, Reaction, And Deactivation Phenomena In The Immobilized Glucose Oxidase And Cataiase System. Biotechnol. Bioeng. 1979; 21: 2061–87
   Google Scholar
• Royer G. P. The Kinetics Of Immobilized Enzymes. Immobilized Enzymes, Antigens, Antibodies, and Peptides, H. H. Weetall. Marcel Dekker, New York 1975; 49, Chapter 2
   Google Scholar
• Royer G. P., Green G. M. Immobilized Pronase. Biochim. Biophys. Res. Commun. 1971; 44: 426–32
   PubMed Web of Science ®Google Scholar
• Royer G. P., Andrews J. P. Immobilized Derivatives Of Leucine Aminopeptidase and Aminopeptidase M. J. Biol. Chem. 1973; 248: 1807–12
   PubMedGoogle Scholar
• Sadana A. Effect Of Immobilized Enzyme Deactivation In Fixed- And Fluid-Bed Reactors. Biotechnol. Bioeng. 1978; 20: 781–97
   Google Scholar
• Sadana A. A Generalized Optimum Temperature Operations Criterion For Deactivating Immobilized Enzyme Batch Reactors. AIChE J. 1979; 25: 535–9
   Google Scholar
• Sadana A. On Optimum Temperature Operations In Deactivating Fixed-Bed Reactors. Chem. Eng. Commun. 1980; 4: 51–5
   Web of Science ®Google Scholar
• Sadana A. A Theoretical Analysis Of The Deactivation Of an Immobilized Enzyme In Multi-Enzyme Reactions In Fixed-Bed and Fluid-Bed Reactors. J. Chem. Tech. Biotechnol. 1981; 31: 553–64
   Google Scholar
• Sadana A. The Optimum Temperature Policy For A deactivating Catalytic Packed-Bed Reactor. An Improved Method Of Operations. Chem. Eng. Sci. 1982; 37: 492–4
   Google Scholar
• San K. Y., Stephanopoulos G. Optimal Control Policy For Substrate Inhibited Kinetics With Enzyme Deactivation In An Isothermal CSTR. AlChE J. 1983; 299: 417–24
   Google Scholar
• Scrutton M. C., Utter M. F. Pyruvate Carboxylase. J. Biol. Chem. 1965; 240: 3714–23
   PubMedGoogle Scholar
• Segel I. H. Enzyme Kinetics—Behavior And Analysis Of Rapid Equilibrium And Steady-State Enzyme Systems. Wiley, New York 1975
   Google Scholar
• Sharp A. K., Kay G., Lilly M. D. The Kinetics Of β-Galactosidase Attached To Porous Cellulose Sheets. Biotechnol. Bioeng. 1969; 11: 363–80
   PubMed Web of Science ®Google Scholar
• Silman I. H., Karlin A. Effect Of Local pH Changes Caused By Substrate Hydrolysis On The Activity Of Membrane-Bound Acetylcholinesterase. Proc. Natl. Acad. Sci. U.S. 1967; 58: 1664–72
   PubMed Web of Science ®Google Scholar
• Staub M. C., Denes G. A Kinetic Study On The Inactivation Of 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate Synthase By Bromopyruvate. Biochim. Biophys. Acta 1967; 139: 519–21
   Google Scholar
• Stone I. 1955, U.S. Patent, 2,717,852
   Google Scholar
• Sudina G. F., Kobelkov G. M., Varfolomeev S. D. The Macrokinetics Of An Enzymatic System Containing An Enzyme That Inactivates In The Course Of Reaction. Biotechnol. Bioeng. 1983; 25: 2519–30
   Google Scholar
• Suzuki H., Ozawa Y., Maeda H. Water-Insoluble Enzyme. Hydrolysis Of Sucrose By Insoluble Yeast Invertase. Agric. Biol. Chem. 1966; 30: 807–13
   Web of Science ®Google Scholar
• Szepe S. The Deactivation Of Catalysts And Some Related Optimization Problems. Ph.D. Thesis, Illinois Institute of Technology, Chicago 1966
   Google Scholar
• Szepe S., Levenspiel O. Optimal Temperature Policies For Reactors Subject To Catalyst Deactivation-I Batch Reactor. Chem. Eng. Sci. 1968; 23: 881–94
   Web of Science ®Google Scholar
• Szepe S., Levenspiel O. Catalyst Deactivation. Fourth European Symposium On Chemical Reaction Engineering. Pergamon Press, Oxford 1971; 265
   Google Scholar
• Thiele F. W. Relation Between Catalytic Activity And Size Of Particle. Ind. Eng. Chem. 1939; 31: 916–20
   Google Scholar
• Tosa T., Mori T., Chibata I. Continuous Enzyme Reactions. VI. Enzyme Properties Of The DEAE-Sephadex-Aminoacylase Complex. Enzymologia 1971; 40: 49–56
   PubMedGoogle Scholar
• Verhoff F. H., Goldstein W. E. Diffusion Resistance And Enzyme Activity Decay In A Pellet. Biotechnol. Bioeng. 1982; 24: 703–23
   PubMed Web of Science ®Google Scholar
• Villadsen J., Stewart W. E. Solution Of Boundary Value Problems By Orthogonal Collocation. Chem. Eng. Sci. 1967; 22: 1483–1501
   Web of Science ®Google Scholar
• Weekman V. W., Jr. A Model Of Catalytic Cracking Conversion In Fixed, Moving and Fluid-Bed Reactors. Ind. Eng. Chem. Process Design Dev. 1968; 7: 90–5
   Web of Science ®Google Scholar
• Weetall H. H. Storage Stability Of Water-Insoluble Enzymes Covalently Coupled To Organic And Inorganic Carriers. Biochim. Biophys. Acta 1970; 212: 1–7
   PubMed Web of Science ®Google Scholar
• Wheeler A. Reaction Rates and Selectivity In Catalyst Pores. Adv. Catalysis 1950; 3: 250–327
   Google Scholar
• Wilson R. J. H., Kay G., Lilly M. D. The Preparation And Kinetics Of Lactate Dehydrogenase Attached To Water-Insoluble Particles And Sheets. Biochem. J. 1968; 108: 845–53
   PubMedGoogle Scholar
• Zaborsky O. R. Alteration Of Enzymic Properties Prior To Immobilization. Food Prod. Dev. 1973; 7: 94–102
   Google Scholar
• Zabriskie D., Ollis D. F., Burger M. M. Activity and Specificity Of Covalently Immobilized Wheat Germ Agglutinin Toward Cell Surfaces. Biotechnol. Bioeng. 1973; 15: 981–92
   Google Scholar
• Zeldovitch I. B. Theory Of Reactions On Powders And Porous Substances. Zh. Fiz. Khim. 1939; 13: 163–8
   Google Scholar