Biotechnology and Bioengineering Author Index to Volume 48 Allen, D. G. See Mohseni, M., 257 a-amylase by Reversed Micellar Temperature on Reaction Kinetics and Anand, S. Extraction, 745 General Considerations of Stability and —; Wu, J.-H.; Diamond, S. L.: Chang, T. M. S. See Lloyd-George, I., Productivity, 190 Enzyme-Mediated Proteolysis of Fibrous 706 Biopolymers: Dissolution Front Chang, Y.-H. D. Das, K. Movement in Fibrin or Collagen Under —,; Grodzinsky, A. J.; Wang, D. I C.: —; Anis, M.; Azemi, B. M. N. M.; Ismail, Conditions of Diffusive or Convective Augmentation of Mass Transfer N.: Fermentation and Recovery of Transport, 89 Through Electrical Means for Glutamic Acid from Palm Waste Anis, M. See Das, K., 551 Hydrogel-Entrapped Escherichia coli Hydrolysate by Ilon-Exchange Resin Arnold, F. H. See Sundaresan, V., 431 Cultivation, 149 Column, 551 —; See Johnson, R. D., 437 Chang, Y. K. Daun, G. See Charcosset, C., 415 Asai, S. See Konishi, Y., 592 —+; McCreath, G. E.; Chase, H. A.: de Gooijer, C. D. See Martens, D. E., 49 Asenjo, J. A. See Kaul, A., 246 Development of an Expanded Bed del Rio, G. Azemi, B. M. N. M. See Das, K., 551 Technique for an Affinity Purification —+; Rodriguez, M.-E.; Munguia, M.-E.; of G6PDH from Unclarified Yeast Cell Lépez-Munguia, A.; Sober6n, X.: Baines, A. J. See Hooker, A. D., 639 Homogenates, 355 Mutant Escherichia coli Penicillin Banik, G. G. Charcosset, C. Acylase with Enhanced Stability at -—; Heath, C. A.: Hybridoma Growth and —,; Su, Z.; Karoor, S.; Daun, G.; Colton, Alkaline pH, 141 Antibody Production as a Function of C. K.: Protein A Immunoaffinity Dhal, P. K. See Sundaresan, V., 431 Cell Density and Specific Growth Rate Hollow Fiber Membranes for Diamond, S. L. See Anand, S., 89 in Perfusion Culture, 289 Immunoglobulin G Purification: Dormish, J. J. See Manning, M. C., 506 Bayne, S. See Mollerup, I., 501 Experimental Characterization, 415 Ducret, A. Belfort, G. See Mallubhotla, H., 375 Chase, H. A. See McCreath, G. E., 341 —,; Giroux, A.; Trani, M.; Lortie, R.: Betenbaugh, M. J. See Tsai, A. M., 715 —,; See Chang, Y. K., 355 Enzymatic Preparation of Biosurfactants Beuvery, E. C. See Martens, D. E., 49 Chattopadhyay, D. from Sugars or Sugar Alcohols and Bhalerao, N. See Gu, T., 520 —,; Rathman, J. F.; Chalmers, J. J.: Fatty Acids in Organic Media Under Blackie, J. D. See Ozturk, S. S., 201 Thermodynamic Approach to Explain Reduced pressure, 214 Boor, R. See Carlson, A., 303 Cell Adhesion to Air-Medium Duine, J. A. See van Tol, J. B. A., 179 Boraschi, D. See Maurizi, G., 197 Interfaces, 649 Borchardt, R. T. See Li, S., 490 Chen, C.-I. Evans, L. L. Bossi, P. See Maurizi, G., 197 —,; Taylor, R. T.: Thermophilic —,; Burns, M. A.: Countercurrent Gradient Bowen, W. R. Biodegradation of BTEX by Two Chromatography: A Continuous —; Moran, E. B.: Ion Exchange of Amino Thermus Species, 614 Focusing Technique, 461 Acids at a Natural Organic Ion Chen, J.-Y. See Chang, Q.-L., 745 Exchanger: Thermodynamics and Chen, W. Y. See Gu, T., 520 Fagervik, K. See von Schalien, R., 631 Energetics, 559 Cheng, C. H. K. See Kwok, F., 542 Fane, A. G. See Liew, M. K. H., 108 Buckland, B. See Lee, S. S., 386 Clonis, Y. D. See Labrou, N. E., 278 Fiers, W. See Steidler, L., 667 Buffiére, P. Colton, C. K. See Charcosset, C., 415 Fonade, C. See Buffiére, P., 725 —,; Stever, J.-P.; Fonade, C.; Moletta, R.: Cramer, S. M. See Kundu, A., 452 Fréchet, J. M. J. See Svec, F., 476 Comprehensive Modeling of Crecchio, C. French, A. D. See Weimer, P. J., 169 Methanogenic Biofilms in Fluidized Bed —,; Ruggiero, P.; Pizzigallo, M. D. R.: Systems: Mass Transfer Limitations and Polyphenoloxidases Immobilized in Gainer, J. L. See Zaidi, A., 601 Multisubstrate Aspects, 725 Organic Gels: Properties and Gao, J. See Skeen, R. S., 659 Bujalski, W. See Priede, M. A., 266 Applications in the Detoxification of Geladé, E. F. T. See van Tol, J. B. A., Bull, A. T. See Hooker, A. D., 639 Aromatic Compounds, 585 179 Bulstra, D. J. See Smolders, G. J. F., 234 Crooks, G. E. Giroux, A. See Ducret, A., 214 Burns, M. A. See Evans, L. L., 461 —,; Rees, G. D.; Robinson, B. H.; Goldman, M. H. See Hooker, A. D., 639 Burt, A. See Lee, S. S., 386 Svensson, M.; Stephenson, G. R.: Gordillo, M. A. See Montesinos, J. L., Comparison of Hydrolysis and 573 Calandranis, J. See Petrides, D., 529 Esterification Behavior of Humicola Grodzinsky, A. J. See Chang, Y.-H. D., Carlson, A. lanuginosa and Rhizomucor miehei 149 —+; Signs, M.; Liermann, L.; Boor, R.; Lipases in AOT-Stabilized Water-in-Oil Gu, T. Jem, K. J.: Mechanical Disruption of Microemulsions: I. Effect of pH and —+; Zheng, Y.; Gu, Y.; Haldankar, R.; Escherichia coli for Plasmid Recovery, Water Content on Reaction Kinetics, 78 Bhalerao, N.; Ridgway, D.; Wiehl, 303 ; Rees, G. D.; Robinson, B. H.; P. E.; Chen, W. Y.; Kopchick, J. J.: Carpenter, J. F. See Manning, M. C., 506 Svensson, M.; Stephenson, G. R.: Purification of a Pyrogen-Free Human Carta, G. See Zaidi, A., 601 Comparison of Hydrolysis and Growth Hormone Antagonist, 520 Chalmers, J. J. See Chattopadhyay, D., Esterification Behavior of Humicola Gu, Y. See Gu, T., 520 649 lanuginosa and Rhizomucor miehei Chang, Q.-L. Lipases in AOT-Stabilized Water-in-Oil Hackney, J. M. See Weimer, P. J., 169 —; Chen, J.-Y.: Purification of Industrial Microemulsions: II. Effect of Haldankar, R. See Gu, T., 520 Biotechnology and Bioengineering, Vol. 48, Pp. 755-758 (1995) Halkjzr, E. See Mollerup, I., 501 of Nitrobenzene through a Hybrid Liermann, L. See Carlson, A., 303 Hampel, W. A. See Schuster, K. C., 66 Pathway in Pseudomonas putida, 625 Liew, M. K. H. Hanson, R. L. See Nanduri, V. B., 547 —,; Fane, A. G.; Rogers, P. L.: Hydraulic Haynes, C. A. Kamphuis, J. See van Tol, J. B. A., 179 Resistance and Fouling of Microfilters —; Sherwood, C. S.; Turner, R. F. B.: Karagouni, A. See Labrou, N. E., 278 by Candida utilis in Fermentation Characterization of an Karau, A. See Thémmes, J., 367 Broth, 108 Oligonucleotide-Binding Fluorescent Karoor, S. See Charcosset, C., 415 Linden, J. C. See Mirjalili, N., 123 Ligand for Application in Affinity Kaul, A. Lloyd-George, I. Purification of dsDNA, 25 —; Pereira, R. A. M.; Asenjo, J. A.; —+; Chang, T. M. S.: Characterization of Heath, C. A. See Banik, G. G., 289 Merchuk, J. C.: Kinetics of Phase Free and Alginate—Polylysine—Alginate Heijnen, J. J. See Smolders, G. J. F., Separation for Polyethylene Microencapsulated Erwinia herbicola —,; See Smolders, G. J. F., 234 Glycol—Phosphate Two-Phase Systems, for the Conversion of Ammonia, —; See van Gulik, W. M., 681 246 Pyruvate, and Phenol into L-Tyrosine, Hooker, A. D. Kawagoe, M. See Naoe, K., 333 706 —; Goldman, M. H.; Markham, N. H.; Kendrick, B. S. See Manning, M. C., 506 Lo, S. C. L. See Kwok, F., 542 James, D. C.; Ison, A. P.; Bull, A. T.; Kierkels, H. G. T. See van Tol, J. B. A., Lombardo, S. Strange, P. G.; Salmon, I.; Baines, 179 —+; Inampudi, P.; Scotton, A.; Ruezinsky, A. J.; Jenkins, N.: N-Glycans of Kieweg, R. See Schuster, K. C., 66 G.; Rupp, R.; Nigam, S.: Development Recombinant Human Interferon-y Kim, H.-S. See Jung, K.-H., 625 of Surface Swabbing Procedures for a Change During Batch Culture of Kitani, Y. See Omasa, T., 673 Cleaning Validation Program in a Chinese Hamster Ovary Cells, 639 Klop, J. M. See Smolders, G. J. F., 222 Biopharmaceutical Manufacturing Hooker, B. S. See Skeen, R. S., 659 Ko, R. Y. See Nanduri, V. B., 547 Facility, 513 Hsiun, D.-Y. See Jong, J.-Z., 207 Kobayashi, A. See Ohtani, N., 42 Lopez-Munguia, A. See del Rio, G., 141 Hutchinson, C. R. See Scotti, C., 133 Kobayashi, F. See Sawada, T., 719 Lortie, R. See Ducret, A., 214 Kobayashi, K.-y. See Yamazaki, M., 17 Louvel, L. See Vanhoutte, B., | Imai, M. See Naoe, K., 333 Kobayashi, M. See Omasa, T., 673 Lowe, C. R. See McCreath, G. E., 341 Imamura, Y. See Omasa, T., 673 Konishi, Y. Inampudi, P. See Lombardo, S., 513 —+; Yoshida, S.; Asai, S.: Bioleaching of Mallubhotla, H. Inoue, Y. See Ohtani, N., 42 Pyrite by Acidophilic Thermophile —,; Nunes, E.; Belfort, G.: Microfiltration Ismail, N. See Das, K., 551 Acidianus brierleyi, 592 of Yeast Suspensions With Ison, A. P. See Hooker, A. D., 639 Kopchick, J. J. See Gu, T., 520 Self-Cleaning Spiral Vortices: Itoh, Y. Kula, M.-R. See Thémmes, J., 367 Possibilities for a New Membrane —; Ueda, H.; Suzuki, E.: Overexpression Kundu, A. Module Design, 375 of bcl-2, Apoptosis Suppressing Gene: —,; Vunnum, S.; Jayaraman, G.; Cramer, Mandrap, G. See Mollerup, I., 501 Prolonged Viable Culture Period of S. M.: Protected Amino Acids As Manning, M. C. Hybridoma and Enhanced Antibody Novel Low-Molecular-Weight —+; Matsuura, J. E.; Kendrick, B. S.; Production, 118 Displacers in Cation-Exchange Meyer, J. D.; Dormish, J. J.; Vrkljan, Iyer, H. V. Displacement Chromatography, 452 M.; Ruth, J. R.; Carpenter, J. F.; —; Przybycien, T. M.: Metal Affinity Kuwahara, M. See Sawada, T., 719 Shefter, E.: Approaches for Increasing Protein Precipitation: Effects of Mixing, Kwok, F. the Solution Stability of Proteins, 506 Protein Concentration, and Modifiers on —+; Wang, X. H.; Cheng, C. H. K.; Lo, Markham, N. H. See Hooker, A. D., 639 Protein Fractionation, 324 S. C. L.: Large Scale Purification of Martens, D. E. myo-Inositol Monophosphate —; Sipkema, E. M.; de Gooijer, C. D.; Jacobs, R. See Smolders, G. J. F., 234 Phosphatase From Porcine Brains, 542 Beuvery, E. C.; Tramper, J.: James, D. C. See Hooker, A. D., 639 A Combined Cell-Cycle and Metabolic Jayaraman, G. See Kundu, A., 452 Labrou, N. E. Model for the Growth of Hybridoma Jem, K. J. See Carlson, A., 303 —; Karagouni, A.; Clonis, Y. D.: Cells in Steady-State Continuous Jenkins, N. See Hooker, A. D., 639 Biomimetic-Dye Affinity Adsorbents Culture, 49 Johns, M. R. See Judge, R. A., 316 for Enzyme Purification: Application to Matsuura, J. E. See Manning, M. C., 506 Johnson, R. D. the One-Step Purification of Candida Maurizi, G. —; Arnold, F. H.: Multipoint Binding and boidinii Formate Dehydrogenase, 278 —,; Bossi, P.; Boraschi, D.; Ulisse, E.; Heterogeneity in Immobilized Metal Lafuente, J. See Montesinos, J. L., 573 Tagliabue, A.; Ruggiero, P.: Affinity Chromatography, 437 Langer, R. See Shefer, S. D., 36 Sporulation: An Alternative Way to Jong, J.-Z. LaPorte, T. L. See Nanduri, V. B., 547 Recover Recombinant Proteins from —; Hsiun, D.-Y.; Wu, W.-T.; Tzeng, Lee, G. M. See Park, S. Y., 699 Bacillus subtilis, 197 Y.-M.: Fed-batch Culture of Bacillus Lee, J.-Y. See Jung, K.-H., 625 Mawatari, Y. See Naoe, K., 333 thuringiensis for Thuringiensin Lee, S. S. Mayer, H. F. See Schuster, K. C., 66 Production in a Tower Type Bioreactor, —+; Burt, A.; Russotti, G.; Buckland, B.: McCreath, G. E. 207 Microfiltration of Recombinant Yeast —; Chase, H. A.; Owen, R. O.; Lowe, Jongejan, J. A. See van Tol, J. B. A., 179 Cells Using a Rotating Disk Dynamic C. R.: Expanded Bed Affinity Jérdening, H.-J. See Walter, J., 12 Filtration System, 386 Chromatography of Dehydrogenases Jorgensen, T. See Mollerup, I., 501 Lewandowski, Z. See Yang, S., 737 from Bakers’ Yeast Using Dye—Ligand Judge, R. A. Li, S. Perfluoropolymer Supports, 341 —; Johns, M. R.; White, E. T.: Protein —,; Schoneich, C.; Borchardt, R. T.: —+; See Chang, Y. K., 355 Purification by Bulk Crystallization: The Chemical Instability of Protein Merchuk, J. C. See Kaul, A., 246 Recovery of Ovalbumin, 316 Pharmaceuticals: Mechanisms of Meyer, J. D. See Manning, M. C., 506 Jung, K.-H. Oxidation and Strategies for Mirjalili, N. —; Lee, J.-Y.; Kim, H.-S.: Biodegradation Stabilization, 490 —,; Linden, J. C.: Gas Phase Composition AUTHOR INDEX Effects on Suspension Cultures of Taxus Ozturk, S. S. Explosion Pretreatment on Enzymatic cuspidata, 123 —-; Thrift, J. C.; Blackie, J. D.; Naveh, Saccharification of Plant Biomass, 719 Mohseni, M. Real-Time Monitoring of Protein Saxén, B. See von Schalien, R., 631 —,; Allen, D. G.: The Effect of Particle Secretion in Mammalian Cell Schéneich, C. See Li, S., 490 Morphology and Concentration on the Fermentation: Measurement of Schuster, K. C. Directly Measured Yield Stress in Monoclonal Antibodies Using a —,; Mayer, H. F.; Kieweg, R.; Hampel, Filamentous Suspensions, 257 Computer-Controlled HPLC System W. A.; Sara, M.: A Synthetic Medium Moletta, R. See Buffiére, P., 725 (BioCad/RPM), 201 for Continuous Culture of the S-Layer Mollerup, I. Carrying Bacillus stearothermophilus —,; Bayne, S.; Halkjer, E.; Jorgensen, T.; Park, S. Y. PV 72 and Studies on the Influence of Mandrap, G.; Nicolaisen, E. M.; Thim, —; Lee, G. M.: Enhancement of Growth Conditions on Cell Wall L.: The Use of RP-HPLC for Measuring Monoclonal Antibody Production by Properties, 66 Activation and Cleavage of rFVIla Immobilized Hybridoma Cell Culture Scotti, C. During Purification, 501 with Hyperosmolar Medium, 699 —,; Hutchinson, C. R.: Immobilization and Montesinos, J. L. Patel, R. N. See Nanduri, V. B., 547 Properties of Carminomycin —,; Lafuente, J.; Gordillo, M. A.; Valero, Pereira, R. A. M. See Kaul, A., 246 4-O-methyltranferase, the Enzyme F.; Sola, C.: Structured Modeling and Petrides, D. Which Catalyzes the Final Step in the State Estimation in a Fermentation —,; Sapidou, E.; Calandranis, J.: Biosynthesis of Daunorubicin in Process: Lipase Production by Candida Computer-Aided Process Analysis and Streptomyces peucetius, 133 rugosa, 573 Economic Evaluation for Biosynthetic Scotton, A. See Lombardo, S., 513 Moran, E. B. See Bowen, W. R., 559 Human Insulin Production—A Case Shefer, S. D. Mori, Y. See Yamazaki, M., 17 Study, 529 —,; Rosenberger, V.; Vahanian, G.; Wong, Mosterd, F. See van Tol, J. B. A., 179 Pizzigallo, M. D. R. See Crecchio, C., W. T.; Langer, R.: Implantable Hollow Mukhopadhyay, A. 585 Fiber Bioreactor as a Potential —+; Mukhopadhyay, S. N.; Talwar, G. P.: Plunkett, S. D. See Sundaresan, V., 431 Treatment for Hypercholesterolemia: Studies on the Synthesis of BhCG Pons, M. N. See Vanhoutte, B., | Characterization of the Catalytic Unit, Hormone in Vero Cells by Recombinant Priede, M. A. 36 Vaccinia Virus, 158 —,; Vanags, J. J.; Viesturs, U. E.; Tucker, Shefter, E. See Manning, M. C., 506 Mukhopadhyay, S. N. See K. G.; Bujalski, W.; Thomas, C. R.: Shen, H. Mukhopadhyay, A., 158 Hydrodynamic, Physiological, and —; Wang, Y.-T.: Modeling Simultaneous Munguia, M.-E. See del Rio, G., 141 Morphological Characteristics of Hexavalent Chromium Reduction and Fusarium moniliforme in Geometrically Phenol Degradation by a Defined Nakamura, Y. See Sawada, T., 719 Dissimilar Stirred Bioreactors, 266 Coculture of Bacteria, 606 Nanduri, V. B. Przybycien, T. M. See Iyer, H. V., 324 Sherwood, C. S. See Haynes, C. A., 25 —,; Hanson, R. L.; LaPorte, T. L.; Ko, Shiloach, J. See Trinh, L., 401 R. Y.; Patel, R. N.; Szarka, L. J.: Rathman, J. F. See Chattopadhyay, D.., —,; See Tsai, A. M., 715 Fermentation and Isolation of 649 Shintaku, Y. See Naoe, K., 333 C10-Deacetylase for the Production of Rees, G. D. See Crooks, G. E., 78 Shioya, S. See Omasa, T., 673 10-Deacetylbaccatin III from Baccatin —+; See Crooks, G. E., 190 Signs, M. See Carlson, A., 303 Ill, 547 Remaut, E. See Steidler, L., 667 Sipkema, E. M. See Martens, D. E., 49 Naoe, K. Ridgway, D. See Gu, T., 520 Skeen, R. S. —; Shintaku, Y.; Mawatari, Y.; Kawagoe, Ringbom, K. See von Schalien, R., 631 —,; Gao, J.; Hooker, B. S.: Kinetics of M.; Imai, M.: Novel Function of Robinson, B. H. See Crooks, G. E., 78 Chlorinated Ethylene Dehalogenation Guanidine Hydrochloride in Reverse —+; See Crooks, G. E., 190 Under Methanogenic Conditions, 659 Micellar Extraction of Lysozyme from Rodriguez, M.-E. See del Rio, G., 141 Smolders, G. J. F. Chicken Egg White, 333 Rogers, P. L. See Liew, M. K. H., 108 —; Klop, J. M.; van Loosdrecht, Naveh, D. See Ozturk, S. S., 201 Rosenberger, V. See Shefer, S. D., 36 M. C. M.; Heijnen, J. J.: A Metabolic Nicolaisen, E. M. See Mollerup, I., 501 Ruezinsky, G. See Lombardo, S., 513 Model of the Biological Phosphorus Nigam, S. See Lombardo, S., 513 Ruggiero, P. See Maurizi, G., 197 Removal Process: I. Effect of the Nishikawa, T. See Omasa, T., 673 —,; See Crecchio, C., 585 Sludge Retention Time, 222 Nunes, E. See Mallubhotla, H., 375 Rupp, R. See Lombardo, S., 513 ; Bulstra, D. J.; Jacobs, R.; van Russotti, G. See Lee, S. S., 386 Loosdrecht, M. C. M.; Heijnen, J. J.: Ruth, J. R. See Manning, M. C., 506 A Metabolic Model of the Biological Ohtani, N. Rydstrém, M. See von Schalien, R., 631 Phosphorus Removal Process: II. —; Inoue, Y.; Kobayashi, A.; Sugawara, Validation During Start-Up Conditions, T.: Transesterification Catalyzed by Sadana, A. 234 Polystyrene-Supported Chymotrypsin in —, Protein Refolding and Inactivation Soberoén, X. See del Rio, G., 141 Toluene: The Effect of Neutralization of During Bioseparation: Bioprocessing Sola, C. See Montesinos, J. L., 573 Basic or Acidic Groups Attaching to Implications, 481 Steidler, L. Polystyrene Resins, 42 Saksena, S. See van Eijndhoven, —,; Fiers, W.; Remaut, E.: Simultaneous Omasa, T. R. H. C. M., 406 Light Emission from Cloned Vibrio —; Kobayashi, M.; Nishikawa, T.; Shioya, Salmon, I. See Hooker, A. D., 639 fischeri lux Genes and Expression of S.; Suga, K.-i.; Uemura, S.-i.; Kitani, Sapidou, E. See Petrides, D., 529 LamB or LamB-protein A Fusion Y.; Imamura, Y.: Enhancement of Sara, M. See Schuster, K. C., 66 Proteins in Escherichia coli Depends on Antibody Production by Growth Factor Sawada, T. Using a Single Chimeric Operon, 667 Addition in Perfusion and Hollow-Fiber —,; Nakamura, Y.; Kobayashi, F.; Stephenson, G. R. See Crooks, G. E., 78 Culture Systems, 673 Kuwahara, M.; Watanabe, T.: Effects —; See Crooks, G. E., 190 Owen, R. O. See McCreath, G. E., 341 of Fungal Pretreatment and Steam Stever, J.-P. See Buffiére, P., 725 AUTHOR INDEX Strange, P. G. See Hooker, A. D., 639 Ueda, H. See Itoh, Y., 118 Walter, J. Su, Z. See Charcosset, C., 415 Uemura, S.-i. See Omasa, T., 673 —, Jérdening, H.-J.: Kinetic Model of Suga, K.-i. See Omasa, T., 673 Ulisse, E. See Maurizi, G., 197 Disaccharide Oxidation by Sugawara, T. See Ohtani, N., 42 Agrobacterium tumefaciens, 12 Sundaresan, V. Wang, D. I C. See Chang, Y.-H. D., 149 —; Dhal, P. K.; Plunkett, S. D.; Arnold, Vahanian, G. See Shefer, S. D., 36 Wang, X. H. See Kwok, F., 542 F. H.: Selective Ligand-Exchange Valero, F. See Montesinos, J. L., 573 Wang, Y.-T. See Shen, H., 606 Adsorbents Prepared by Template van der Tweel, W. J. J. See van Tol, Watanabe, T. See Sawada, T., 719 Polymerization, 431 J. B. A., T9 Weiher, M. See Thémmes, J., 367 Suzuki, E. See Itoh, Y., 118 van Eijndhoven, R. H. C. M. Weimer, P. J. Svec, F. —,; Saksena, S.; Zydney, A. L.: Protein —+; Hackney, J. M.; French, A. D.: Effects —,; Fréchet, J. M. J.: ‘‘Molded’’ Rods of Fractionation Using Electrostatic of Chemical Treatments and Heating on Macroporous Polymer for Preparative Interactions in Membrane Filtration, 406 the Crystallinity of Celluloses and Their Separations of Biological Products, 476 van Gulik, W. M. Implications for Evaluating the Effect of Svensson, M. See Crooks, G. E., 78 —+; Heijnen, J. J.: A Metabolic Network Crystallinity on Cellulose —; See Crooks, G. E., 190 Stoichiometry Analysis of Microbial Biodegradation, 169 Szarka, L. J. See Nanduri, V. B., 547 Growth and Product Formation, 681 White, E. T. See Judge, R. A., 316 van Loosdrecht, M. C. M. See Smolders, Wiehl, P. E. See Gu, T., 520 Tagliabue, A. See Maurizi, G., 197 G. 3. F.,. a Wong, W. T. See Shefer, S. D., 36 Takezawa, T. See Yamazaki, M., 17 —+; See Smolders, G. J. F., 234 Wu, J.-H. See Anand, S., 89 Talwar, G. P. See Mukhopadhyay, A.., van Tol, J. B. A. Wu, W.-T. See Jong, J.-Z., 207 158 —; Jongejan, J. A.; Duine, J. A.; Kierkels, Taylor, R. T. See Chen, C.-I., 614 H. G. T.; Geladé, E. F. T.; Mosterd, Yamamoto, S. Thim, L. See Mollerup, I., 501 F.; van der Tweel, W. J. J.; Kamphuis, —,; Plate Height Determination for Gradient Thomas, C. R. See Vanhoutte, B., | J.: Thermodynamic and Kinetic Elution Chromatography of Proteins, —; See Priede, M. A., 266 Parameters of Lipase-Catalyzed Ester 444 Thémmes, J. Hydrolysis in Biphasic Systems with Yamazaki, M. —; Weiher, M.; Karau, A.; Kula, M.-R.: Varying Organic Solvents, 179 —+; Tsuchida, M.; Kobayashi, K.-y.; Hydrodynamics and Performance in Vanags, J. J. See Priede, M. A., 266 Takezawa, T.; Mori, Y.: A Novel Fluidized Bed Adsorption, 367 Vanhoutte, B. Method to Prepare Multiceliular Thrift, J. C. See Ozturk, S. S., 201 —,; Pons, M. N.; Thomas, C. R.; Louvel, Spheroids from Varied Cell Types, 17 Tramper, J. See Martens, D. E., 49 L.; Vivier, H.: Characterization of Yang, S. Trani, M. See Ducret, A., 214 Penicillium chrysogenum Physiology in —; Lewandowski, Z.: Measurement of Trinh, L. Submerged Cultures by Color and Local Mass Transfer Coefficient in —+; Shiloach, J.: Recovery of Insect Cells Monochrome Image Analysis, | Biofilms, 737 Using Hollow Fiber Microfiltration, 401 Viesturs, U. E. See Priede, M. A., 266 Yoshida, S. See Konishi, Y., 592 Tsai, A. M. Vivier, H. See Vanhoutte, B., | —; Betenbaugh, M. J.; Shiloach, J.: The von Schalien, R. Zaidi, A. Kinetics of RCC1 Inclusion Body —, Fagervik, K.; Saxén, B.; Ringbom, K.; —; Gainer, J. L.; Carta, G.: Fatty Acid Formation in Escherichia Coli, 715 Rydstré6m, M.: Adaptive On-line Model Esterification Using Nylon-Immobilized Tsuchida, M. See Yamazaki, M., 17 for Aerobic Saccharomyces cerevisiae Lipase, 601 Tucker, K. G. See Priede, M. A., 266 Fermentation, 631 Zheng, Y. See Gu, T., 520 Turner, R. F. B. See Haynes, C. A., 25 Vrkijan, M. See Manning, M. C., 506 Zydney, A. L. See van Eijndhoven, Tzeng, Y.-M. See Jong, J.-Z., 207 Vunnum, S. See Kundu, A., 452 R. H. C. M., 406 AUTHOR INDEX Biotechnology and Bioengineering Subject Index to Volume 48 a-amylase, 745 CHO cells, 639 Glucose, 207 Acidianus brierleyi, 592 Chromatography, 437, 461 Glutamic acid fermentation, 551 Acidophilic thermophile, 592 Chromatography, displacement, 452 Glycosylation, 639 Activation, 501 Chromium reduction, 606 G6PDH, 355 Activity coefficient, 179 Chromosome condensation protein, 715 Gradient elution, 444 Adsorption, 367 Cleaning validation, 513 Gradient surface, 17 Adsorption, heterogeneous, 437 Cleavage, 501 Growth factor, 673 Affinity chromatography, 278, 341 Coculture, 606 Growth rate, 289 Affinity membranes, 415 Collagen, 17, 89 Guanidine hydrochloride, 333 Albumin, 406 Colloidal suspension, 375 Aliquat 336, 745 Concentration polarization, 375 Hemoglobin, 406 Amino acid, 452 Contaminant recovery, 513 Hexopyranoside:cytochrome c Amino acids, 559 Continuous medium, 476 oxidoreductase, 12 6-amino-penicillanic acid, 141 Countercurrent gradient chromatography, Hollow fiber, 36, 401 Ammonia conversion, 706 461 Hollow-fiber culture, 673 Anaerobic digestion, 725 Crosslinkage, 17 Human growth hormone, 520 Animal cell culture, 520 Crystal growth rate, 316 Human insulin, biosynthetic process design, Antibody production rate, 673 Crystalline surface layers, 66 529 Antibody productivity, 118, 699 Crystallinity, 169 Human serum albumin, 461 Apoptosis, 49, 118 Humicola lanuginosa, 78, 190 Aromatic hydrocarbon, 614 Hybrid strain, 625 Daunorubicin biosynthesis, 133 Hybridoma, 49, 118, 289, 699 10-Deacetylbaccatin III, 547 BhCG, 158 Dechlorination, 659 Hydraulic resistance, 108 B. subtilis, 197 Dehydrogenases, 341 Hydrodynamics, 266, 367 Baccatin III, 547 Denaturation, 506 Hydrolysis, 78, 179, 190 Bacillus stearothermophilus, 66 Depressurization, 108 Hyperosmotic stress, 699 Bacillus thuringiensis, 207 Diafiltration, 406 Baker’s yeast, 355 Differentiation, | IgG, 415 bel-2, 118 Diffusion, 89 IgG-binding protein A domains, 667 Biocatalysis, 141 Disaccharide oxidation, 12 Image analysis, 1, 266 Biodegradation, 169, 614, 625 DNA purification, 25 Immobilization, 699 Biofilm, 737 DNA-binding fluorophore, 25 Immobilized enzymes, 36 Biofilms, 725 Dye-ligand, 341 Immunoadsorption, 415 Bioleaching, 592 Dye-ligand affinity purification, 355 Immunological and biological activity, 158 Biomass yield, 681 Inclusion body, 715 Biomimetic dye, 278 Inositol monophosphatase, 542 Bioreactor, 36 Economic evaluation, 529 Insect cells, 401 Bioseparation, 481 Electrostatic interactions, 406 Insulin, 529 Biotic detoxification, 585 Enzymatic hydrolysis, 551 Interfacial tension, 649 Biphasic system, 179 Enzymatic reaction, 42 Interferon, 639 Bovine serum albumin, 673 Enzymatic saccharification, 719 Ion exchange, 559 BTEX, 614 Enzyme immobilization, 133, 585, 601 Ion-exchange chromatography, 444 Bulk crystallization, 316 Enzyme kinetics, 133 lon-exchange resin column, 551 Enzyme purification, 278 Escherichi coli, 149 Kinetic data analysis, 706 Candida antarctica, 214 Escherichia coli, 303, 606, 667, 715 Kinetic energy, 266 Candida boidinii, 278 Esterification, 78, 190, 601 Kinetic model, 12 Candida rugosa, 573 Ethylene, 123, 659 Kinetics, 501 Candida utilis, 681 Expanded bed, 341 Carbon analysis, 513 Expanded beds, 355 Carbon dioxide, 123 LamB fusions, 667 Extraction, 333 Cation exchange systems, 452 Light emission, 667 C10-deacetylase, 547 Lipase, 214, 573, 601 Cell adhesion, 649 Fatty acid, 601 Liquid chromatography, 476 Cell cultures, 149 Fermentation, 12, 547, 573, 631 Lithium, 542 Cell cycle, 49 Fibrin, 89 Low density lipoprotein, 36 Ceil density, 289 Filamentous Fermentation Broths, 257 Lysozyme, 333 Cell disruption, 303 Filtration, 386 Cell lysis, 197 Fluidization, 367 Macroporous polymer, 476 Cell survival, 118 Fluorescent ligand, 25 Mammalian cell culture fermentation, 201 Cellulose, 169 Formate dehydrogenase, 278 Mass spectrometry, 639 Chelator, 490 Fouling, 108, 375 Mass transfer, 149 Chicken egg white, 333 Fungal treatment, 719 Mass transfer coefficient, 737 Chimeric operon, 667 Fusarium moniliforme, 266 Membrane filtration, 406 Biotechnology and Bioengineering, Vol. 48, Pp. 759-760 (1995) Membrane microfiltration, 375 PHB, 234 Rhizomucor miehei, 78, 190 Metabolic fluxes, 681 PHB, glycogen, 222 RP-HPLC, 501 Metabolic model, 222, 234 Phenoloxidases, 585 . Metabolism, 614 Phosphate, 246 Saccharomyces cerevisiae, 386, 631, 681 Metal affinity, 324 Phospholipase A,, 36 Secondary metabolite, 123 Metal affinity chromatography, 437 Phosphorus removal, biological, 222, 234 Self-cleaning spiral vortices, 375 Metal catalysis, 490 Photooxidation, 490 Serum, 520 Metal recovery, 592 Physiology, | Solvation, 179 Metal-ligand coordination, 431 Plant biomass, 719 Spheroid, 17 Methanogenic activity, 659 Plasma fractionation, 324 Sporulation, 197 Microcalorimetry, 559 Plasmid recovery, 303 Start-up, 234 Microelectrode, 737 Plasminogen, 89 State estimation, 631 Microencapsulation, 706 Polyethylene glycol, 246 Steam explosion, 719 Microfiltration, 108, 386, 401 Polymer, temperature-responsive, 17 Stirred bioreactor, 266 Microheterogeneity, 639 Polyphosphate, 222, 234 Stoichiometry, 681 Mixing, 324 Polystyrene-immobilized a-chymotrypsin, STREAMLINE red H-E7B, 355 Modeling, 573 42 Streptomyces peucetius, 133 MOI, 158 Porosity, 36 Structured modeling, 573 Molded column, 476 Preparative HPLC, 476 Sugar esters, 214 Molecular imprinting, 431 Preparative separation, 444 Surface modification, 431 Molecular recognition, 431 Procion red H-E7B, 355 Synthetic medium, 66 Monoclonal antibodies, 201 Product recovery, 551 Monoclonal antibody, 289 Product yield, 681 Taxol, 123 Morphology, 257, 266 Protein, 490 Taxus cuspidata, 123 mRNA, 158 Protein A, 415 Thermodynamic model, 649 Protein binding, 437 Thermodynamics, 559 Neutralized supports, 42 Protein precipitation, 324 Thermophile, 614 n-hexane, 601 Protein purification, 367, 452 Thermus, 614 Nitrobenzene, 625 Protein refolding, 481 Thuringiensin production, 207 Nocardioides luteus, 547 Protein separation, 444, 461 Toluene, 42 Nonaqueous media, 214 Protein separations, 406 Transesterification, 42 Nucleation, 316 Protein stability, 141 Triazine dye, 278 Protein stabilization, 506 Tyrosine phenol-lyase, 706 On-line simulation, 631 Protein surface charge, 141 Tyrosine production, 706 Organic gels, 585 Proteins, 476 Organic solvents, 179 Proteolysis, 89 Urokinase, 506 Ovalbumin, 316 Pseudomonas putida, 606 Vaccinia virus expression, 158 Oxidation, 12, 490 Purification, 316, 520, 542, 745 Vero, 158 Oxygen, 123 Pyrite, 592 Vibrio fischeri lux genes, 667 Penicillium chrysogenum, | Recombinant protein purification, 197 Wastewater treatment, 725 Peptide, 490 Reverse micelle, 333 Perfluoropolymers, 341 Reverse micelles, 481, 585 x-ray diffraction, 169 Perfusion, 289 Reversed micelles, 745 Perfusion culture, 673 rFVIla, 501 Yeast, 108, 375, 386 Phase separation, 246 Rheology, 257 Yield stress, 257 SUBJECT INDEX