Harvey W. Blanch

University of California, Riverside

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Douglas S. Clark

University of California, Berkeley

119

John M. Prausnitz

University of California, Berkeley

Elmer Gaden

Columbia University

Eleftherios T. Papoutsakis

Northwestern University

Maria‐Regina Kula

Heinrich Heine University Düsseldorf

Arnold L. Demain

Drew University

James E. Bailey

University of Tennessee Health Science Center

C. R. Wilke

TU Bergakademie Freiberg

C. P. Leslie Grady

Clemson University

Michael L. Shuler

Cornell University

Cooperative Institutions

University of California, Berkeley

241

Lawrence Berkeley National Laboratory

John Wiley & Sons (United States)

Bioengineering Center

University of California System

Massachusetts Institute of Technology

National Center for Genetic Engineering and Biotechnology

University of Virginia

Northwestern University

Stadtwerke Jülich (Germany)

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Swelling equilibria for positively ionized polyacrylamide hydrogels

Macromolecules (1990)

Herbert H. Hooper John P. Baker Harvey W. Blanch John M. Prausnitz

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSwelling equilibria for positively ionized polyacrylamide hydrogelsHerbert H. Hooper, John P. Baker, Harvey W. Blanch, and John M. PrausnitzCite this: Macromolecules 1990, 23, 4, 1096–1104Publication Date (Print):February 1, 1990Publication History Published online1 May 2002Published inissue 1 February 1990https://pubs.acs.org/doi/10.1021/ma00206a031https://doi.org/10.1021/ma00206a031research-articleACS PublicationsRequest reuse permissionsArticle Views1755Altmetric-Citations212LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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10.1021/ma00206a031

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Citations (231)

Techno-Economic Modeling of Cellulosic Biorefineries

Daniel Klein‐Marcuschamer Piotr Oleśkowicz-Popiel Blake A. Simmons Harvey W. Blanch

Author(s): Klein-Marcuschamer, Daniel; Oleskowicz-Popiel, Piotr; Simmons, Blake A.; Blanch, Harvey W.

Cellulosic ethanol

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Possible Taxonomic Trends in the Success of Primary Aggregate Formation in Marine Sponge Cell Cultures

Marine Biotechnology (2008)

Bradley M. Holmes Harvey W. Blanch

Sponge

10.1007/s10126-007-9047-8

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Citations (3)

Pore-size distributions of cationic polyacrylamide hydrogels of different compositions maintained at the same swelling capacity

Journal of Macromolecular Science Part B (1994)

Dieter H. Walther Garrett H. Sin Harvey W. Blanch John M. Prausnitz

Abstract Pore-size distributions have been measured for cationic acrylamide-based hydrogels of different compositions maintained at the same swelling capacity (27.8 ± 0.7 g swollen gel/g dry gel) by varying the ionic strength of the surrounding solution. Swelling equilibria were measured at about 6°C in pure water and aqueous sodium azide solutions ranging in concentration from to 10−3 to 10−1 M. The mixed-solute-exclusion method (introduced by Kuga) was used to obtain the experimental solute-exclusion curve, which represents the amount of imbibed liquid inside the gel inaccessible to a solute of radius r. The pore-size distribution was obtained by using Casassa's Brownian-motion model and numerically solving the Fredholm integral equation. The modes of the pore radii range from 20.4 to 47.1 Å for acrylamide-based hydrogels containing varying amounts of cationic comonomer (1.5 and 4.0 %M), crosslinker (0.3 and 1.0 %C), and initial concentration of total monomer (15 and 35 % T).

Cationic polymerization

Polyacrylamide

Comonomer

10.1080/00222349408248092

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Citations (7)

A kinetic analysis of hybridoma growth and metabolism in batch and continuous suspension culture: Effect of nutrient concentration, dilution rate, and pH

Biotechnology and Bioengineering (1988)

William M. Miller Harvey W. Blanch C. R. Wilke

Hybridomas are finding increased use for the production of a wide variety of monoclonal antibodies. Understanding the roles of physiological and environmental factors on the growth and metabolism of mammalian cells is a prerequisite for the development of rational scale-up procedures. An SP2/0-derived mouse hybridoma has been employed in the present work as a model system for hybridoma suspension culture. In preliminary shake flask studies to determine the effect of glucose and glutamine, it was found that the specific growth rate, the glucose and glutamine metabolic quotients, and the cumulative specific antibody production rate were independent of glucose concentration over the range commonly employed in cell cultures. Only the specific rate of glutamine uptake was found to depend on glutamine concentration. The cells were grown in continuous culture at constant pH and oxygen concentration at a variety of dilution rates. Specific substrate consumption rates and product formation rates were determined from the steady state concentrations. The specific glucose uptake rate deviated from the maintenance energy model(1) at low specific growth rates, probably due to changes in the metabolic pathways of the cells. Antibody production was not growth-associated; and higher specific antibody production rates were obtained at lower specific growth rates. The effect of pH on the metabolic quotients was also determined. An optimum in viable cell concentration was obtained between pH 7.1 and 7.4. The viable cell number and viability decreased dramatically at pH 6.8. At pH 7.7 the viable cell concentration initially decreased, but then recovered to values typical of pH 7.1-7.4. Higher specific nutrient consumption rates were found at the extreme pH values; however, glucose consumption was inhibited at low pH. The pH history also influenced the behavior at a given pH. Higher antibody metabolic quotients were obtained at the extreme pH values. Together with the effect of specific growth rate, this suggests higher antibody production under environmental or nutritional stress.

Dilution

10.1002/bit.260320803

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Citations (478)

Biodesulfurization of dibenzothiophene in Escherichia coli is enhanced by expression of a Vibrio harveyi oxidoreductase gene

Biotechnology and Bioengineering (2000)

David. Reichmuth Jessica L. Hittle Harvey W. Blanch Jay D. Keasling

One possible alternative to current fuel hydrodesulfurization methods is the use of microorganisms to remove sulfur compounds. Biodesulfurization requires much milder processing conditions, gives higher specificity, and does not require molecular hydrogen. In the present work we have produced two compatible plasmids: pDSR3, which allows Escherichia coli to convert dibenzothiophene (DBT) to hydroxybiphenyl (HBP), and pDSR2, which produces a Vibrio harveyi flavin oxidoreductase. We show that the flavin oxidoreductase enhances the rate of DBT removal when co-expressed in vivo with the desulfurization enzymes. The plasmids pDSR2 and pDSR3 were co-expressed in growing cultures. The expression of oxidoreductase caused an increase in the rate of DBT removal but a decrease in the rate of HBP production. The maximum rate of DBT removal was 8 mg/h · g dry cell weight. Experiments were also conducted using resting cells with the addition of various carbon sources. It was found that the addition of glucose or glycerol to cultures with oxidoreductase expression produced the highest DBT removal rate (51 mg/h · g dry cell weight). The culture with acetate and no oxidoreductase expression had the highest level of HBP production. For all carbon sources, the DBT removal rate was faster and the HBP generation rate slower with the expression of the oxidoreductase. Analysis of desulfurization intermediates indicates that the last enzyme in the pathway may be limiting. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 67: 72–79, 2000.

Dibenzothiophene

10.1002/(sici)1097-0290(20000105)67:1<72::aid-bit8>3.3.co;2-3

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Citations (3)

Microbial hollow fiber bioreactors

Trends in biotechnology (1983)

Tania Roy Harvey W. Blanch C. R. Wilke

Hollow fiber membrane

10.1016/0167-7799(83)90003-3

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Citations (50)

Application of MacMillan-Majer Theory to Dilute Liquid Systems

C.A. Haynes J.F. Newman Harvey W. Blanch John M. Prausnitz

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Capillary electrophoresis of DNA in uncrosslinked polymer solutions: Evidence for a new mechanism of DNA separation

Biotechnology and Bioengineering (1996)

Annelise E. Barron Wade M. Sunada Harvey W. Blanch

10.1002/(sici)1097-0290(19961020)52:2<259::aid-bit7>3.3.co;2-#

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Effect of sodium dodecylbenzene sulfonate on subtilisin Carlsberg proteolysis of an immobilized ovalbumin film

Biotechnology and Bioengineering (2008)

Ladan L. Foose Harvey W. Blanch Clayton J. Radke

Enzymatic degradation of immobilized ovalbumin multilayer films by subtilisin Carlsberg was investigated using in situ ellipsometry. Changes in the substrate cleavage rate in the presence of an anionic surfactant, sodium dodecylbenzene sulfonate (SDBS), were assessed. Exposure of the protein film to SDBS prior to introduction of the enzyme increased the measured proteolysis rate threefold. Surfactant increased the measured film thickness, absorbing into the protein film and causing swelling. Surfactant-induced film swelling was reversible upon aqueous rinsing. Nevertheless, exposure of enzyme to the surfactant-rinsed film increased the proteolysis rate, most likely due to irreversible conformational changes induced in the substrate film by the surfactant. Simultaneous addition of SDBS with enzyme after the initial surfactant exposure did not produce additional protein-removal benefit.

Dodecylbenzene

Subtilisin

Proteolysis

10.1002/bit.22144

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Citations (3)