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United States Department of Agriculture

Agricultural Research Service

Related Topics

Douglas B Jordan
Bioenergy Research
General Biological Science

Phone: (309) 681-6472
Fax: (309) 681-6427
Room 2131B

1815 N UNIVERSITY ST
PEORIA , IL 61604

Projects
Technologies for Improving Process Efficiencies in Biomass Refineries
Appropriated (D)
  Accession Number: 427437

Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
Biochemical characterization of a GH43 ß-xylosidase from Bacteroides ovatus -
Expression and characterization of hyperthermostable exo-polygalacturonase TtGH28 from Thermotoga thermophilus -
Wagschal, K.C., Stoller, J.R., Chan, V.J., Lee, C.C., Grigorescu, A.A., Jordan, D.B. 2016. Expression and characterization of hyperthermostable exo-polygalacturonase TtGH28 from Thermotoga thermophilus. Molecular Biotechnology. 58(7):509-519. doi 10.1007/s12033-016-9948-8.
Cloning and divalent-metal activation of a ß-xylosidase, RUM630-BX -
Jordan, D.B., Braker, J.D., Wagschal, K.C., Stoller, J.R., Lee, C.C. 2015. Cloning and divalent-metal activation of a ß-xylosidase, RUM630-BX. Enzyme and Microbial Technology. 82:158.
Rate-limiting steps of stereochemistry retaining ß-D-xylosidase from Geobacillus stearothermophilus acting as substrates Reprint Icon -
Jordan, D.B., Braker, J.D. 2015. Rate-limiting steps of stereochemistry retaining ß-d-xylosidase from Geobacillus stearothermophilus acting on four substrates. Archives of Biochemistry and Biophysics. 583:73-78. doi: 10.1016/j.abb.2015.08.004.
X-ray crystal structure of divalent metal-activated ß-xyloisdase, RS223BX Reprint Icon -
Jordan, D.B., Braker, J.D., Wagschal, K., Lee, C.C., Chan, V.J., Dubrovska, I., Anderson, S., Wawrzak, Z. 2015. X-ray crystal structure of divalent metal-activated ß-xyloisdase, RS223BX. Applied Biochemistry and Biotechnology. 177:637-648. doi: 10.1007/s12010-015-1767-z.
Biochemical characterization of uronate dehydrogenases from three Pseudomonads, Chromohalobacter salixigens, and Polaromonas naphthalenivorans Reprint Icon -
Wagschal, K.C., Jordan, D.B., Lee, C.C., Younger, A.R., Braker, J.D., Chan, V.J. 2014. Biochemical characterization of uronate dehydrogenases from three Pseudomonads, Chromohalobacter salixigens, and Polaromonas naphthalenivorans. Enzyme and Microbial Technology. 69:62-68.
Directed evolution of GH43 ß-xylosidase XylBH43 thermal stability and L186 saturation Reprint Icon -
Singh, S.K., Heng, C., Braker, J.D., Chan, V.J., Lee, C.C., Jordan, D.B., Yuan, L., Wagschal, K.C. 2013. Directed evolution of GH43 ß-xylosidase XylBH43 thermal stability and L186 saturation. Journal of Industrial Microbiology and Biotechnology. 41(3):489-498. doi: 10.1007/s10295-013-1377-0.
Rehabilitation of faulty kinetic determinations and misassigned glycoside hydrolase family of retaining mechanism ß-xylosidases Reprint Icon -
Jordan, D.B., Vermillion, K., Grigorescu, A.A., Braker, J.D. 2013. Rehabilitation of faulty kinetic determinations and misassigned glycoside hydrolase family of retaining mechanism ß-xylosidases. Archives of Biochemistry and Biophysics. 537(2):176-184.
Activation of a GH43 ß-xylosidase by divalent metal cations: Slow binding of divalent metal and high substrate specificity -
Jordan, D.B., Lee, C.C., Wagschal, K., Braker, J.D. 2013. Activation of a GH43 ß-xylosidase by divalent metal cations: Slow binding of divalent metal and high substrate specificity. Archives of Biochemistry and Biophysics. 533:79-87.
Divalent metal activation of a GH43 ß-xylosidase -
Lee, C.C., Braker, J.D., Grigorescu, A.A., Wagschal, K.C., Jordan, D.B. 2013. Divalent metal activation of a GH43 ß-xylosidase. Enzyme and Microbial Technology. 52(2):84-90.
Highly active ß-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates -
Jordan, D.B., Wagschal, K.C., Grigorescu, A.A., Braker, J.D. 2013. Highly active ß-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates. Applied Microbiology and Biotechnology. 97:4415-4428.
Plant cell walls to ethanol. -
Jordan, D.B., Bowman, M.J., Braker, J.D., Dien, B.S., Hector, R.E., Lee, C.C., Mertens, J.A., Wagschal, K.C. 2012. Plant cell walls to ethanol. Biochemical Journal. 442:247-252.
Opposing influences by subsite -1 and subsite +1 residues on relative xylopyranosidase/arabinofuranosidase activities of bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase -
Jordan, D.B., Braker, J.D. 2011. Opposing influences by subsite -1 and subsite +1 residues on relative xylopyranosidase/arabinofuranosidase activities of bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase. Biochimica et Biophysica Acta. 1814:1648-1657.
Kinetic mechanism of an aldehyde reductase of Saccharomyces cerevisiae that relieves toxicity of furfural and 5-hydroxymethylfurfural -
Jordan, D.B., Braker, J.D., Bowman, M.J., Vermillion, K., Moon, J., Liu, Z. 2011. Kinetic mechanism of an aldehyde reductase of Saccharomyces cerevisiae that relieves toxicity of furfural and 5-hydroxymethylfurfural. Biochimica et Biophysica Acta. 1814:1686-1694.
Catalytic properties of ß-D-xylosidase XylBH43 from Bacillus halodurans C-125 and mutant XylBH43-W147G -
Wagschal, K.C., Jordan, D.B., Braker, J.D. 2011. Expression, characterization, and site-directed mutagenesis of ß-D-xylosidase XylBH43 from Bacillus halodurans C-125. Process Biochemistry. doi:10.1016/j.procbio.2011.07.009.
Engineering lower inhibitor affinities in beta-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145 -
Jordan, D.B., Wagschal, K.C., Zhanmin, F., Yuan, L., Braker, J.D., Heng, C. 2011. Engineering lower inhibitor affinities in beta-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145. Journal of Industrial Microbiology and Biotechnology. 38:1821-1835.
Stereochemistry of Furfural Reduction by a Saccharomyces cerevisiae Aldehyde Reductase That Contributes to In Situ Furfural Detoxification -
Bowman, M.J., Jordan, D.B., Vermillion, K., Braker, J.D., Moon, J., Liu, Z. 2010. Stereochemistry of Furfural Reduction by a Saccharomyces cerevisiae Aldehyde Reductase That Contributes to In Situ Furfural Detoxification. Applied and Environmental Microbiology. 76(15):4926-4932.
Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris -
Mertens, J.A., Braker, J.D., Jordan, D.B. 2010. Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris. Applied Biochemistry and Biotechnology. 162(8):2197-2213.
and applications of microbial ß-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium -
Jordan, D.B., Wagschal, K.C. 2010. Properties and applications of microbial beta-D-xylosidases. Applied Microbiology and Biotechnology. 86(6):1647-1658
Engineering lower inhibitor affinities in beta-D-xylosidase by site-directed mutagenesis of Trp 145 -
Jordan, D.B., Wagschal, K.C., Fan, Z., Yuan, L., Braker, J.D., Heng, C. 2010. Engineering lower inhibitor affinities in beta-D-xylosidase by site-directed mutagenesis of Trp 145. Meeting Abstract. 84.
Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-Directed Mutagenesis, Alternate Substrates, and Active-site Inhibitor -
Jordan, D.B., Braker, J.D. 2010. Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-directed Mutagenesis, Alternate Substrates, and Active-site Inhibitor. Applied Biochemistry and Biotechnology. 161(1-8):395-410.
Engineering Lower Inhibitor Affinities in Beta-D-Xylosidase -
Fan, Z., Yuan, L., Jordan, D.B., Wagschal, K.C., Heng, C., Braker, J.D. 2010. Engineering lower inhibitor affinities in beta-D-xylosidase. Applied Microbiology and Biotechnology. 86(4):1099-1113.
Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-directed Mutagenesis, Alternate Substrates, and Inhibitor -
Beta-D-xylosidase from Selenomonas ruminantium: role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and inhibitors -
Hemicellulolytic Enzymes from the Maize Endophyte Acremonium zeae -
Bischoff, K.M., Jordan, D.B., De Rezende, S.T., Rich, J.O. 2009. Hemicellulolytic enzymes from the maize endophyte Acremonium zeae [abstract]. Biotechnology for Fuels and Chemicals. Poster No. 5-57. p. 120.
Extracellular Hemicellulolytic Enzymes from the Maize Endophyte Acremonium zeae -
Bischoff, K.M., Wicklow, D.T., Jordan, D.B., De Rezende, S.T., Liu, S., Hughes, S.R., Rich, J.O. 2009. Extracellular hemicellulolytic enzymes from the maize endophyte Acremonium zeae. Current Microbiology. 58:499-503.
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions -
Jordan, D.B., Braker, J.D. 2009. Beta-D-xylosidase from Selenomonas ruminantium: Thermodynamics of Enzyme-catalyzed and Noncatalyzed Reactions. Applied Biochemistry and Biotechnology. 155(1-3):330-346.
Aminoalcohols as Probes of the Two-subsite Active Site of Beta-D-xylosidase from Selenomonas ruminantium -
Jordan, D.B., Mertens, J.A., Braker, J.D. 2009. Aminoalcohols as Probes of the Two-subsite Active Site of Beta-D-xylosidase from Selenomonas ruminantium. Biochimica et Biophysica Acta. 1794(1):144-158.
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions -
Enzymes, Industrial -
Saha, B.C., Bothast, R.J., Jordan, D.B. 2009. Enzymes, Industrial (Overview). In: Schaechter, M., editor. Encyclopedia of Microbiology. Oxford: Elsevier. p. 281-294.
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions -
Beta-D-xylosidase from Selenomonas ruminantium: catalyzed reactions with natural substrates -
Biofuels Group NSF DUSEL Project -
Bang, S., Sani, R., Bleakly, B., Bischoff, K.M., Hughes, S.R., Wagschal, K.C., Wong, D., Lee, C.C., Jordan, D.B., Pokkuluri, R., Schiffer, M. 2008. Biofuels Group NSF DUSEL Project [abstract]. Homestake DUSEL Spring Workshop. Talk 10. p. 2.
Structure of the two-subsite beta-D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane -
Brunzelle, J.S., Jordan, D.B., McCaslin, D.R., Olczak, A., Wawrzak, Z. 2008. Structure of the two-subsite beta-D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino] propane. Archives Of Biochemistry and Biophysics. 474(1):157-166.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM: CATALYZED REACTIONS WITH NATURAL AND ARTIFICIAL SUBSTRATES -
Jordan, D.B. 2008. Beta-D-xylosidase from Selenomonas ruminantium: catalyzed reactions with natural and artificial substrates. Applied Biochemistry and Biotechnology. 146:137-149.
STRUCTURE-FUNCTION RELATIONSHIPS OF A CATALYTICALLY-EFFICIENT BETA-D-XYLOSIDASE -
VARIATION IN RELATIVE SUBSTRATE SPECIFICTY OF BIFUNCTIONAL BETA-D-XYLOSIDASE/ALPHA-L-ARABINOFURANOSIDASE BY SINGLE-SITE MUTATIONS: ROLES OF SUBSTRATE DISTORTION AND RECOGNITION -
Jordan, D.B., Li, X. 2007. Variation in relative substrate specificity of bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase by single-site mutations: roles of substrate distortion and recognition. Biochimica et Biophysica Acta. 1774(9):1192-1198.
INHIBITION OF THE TWO-SUBSITE BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM BY SUGARS: COMPETITIVE, NONCOMPETITIVE, DOUBLE BINDING, AND SLOW BINDING MODES -
Jordan, D.B., Braker, J.D. 2007. Inhibition of the two-subsite beta-d-xylosidase from Selenomonas ruminantium by sugars: competitive, noncompetitive, double binding, and slow binding modes. Archives of Biochemistry and Biophysics. 465(1):231-246.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM: THERMODYNAMICS OF ENZYME-CATALYZED AND NONCATALYZED REACTIONS -
Jordan, D.B. 2007. Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions [abstract]. Biotechnology for Fuels and Chemicals. p. 105.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM: CATALYZED REACTIONS WITH NATURAL AND ARTIFICIAL SUBSTRATES -
Jordan, D.B. 2007. Beta-D-xylosidase from Selenomonas ruminantium: catalyzed reactions with natural and artificial substrates [abstract]. Biotechnology for Fuels and Chemicals. p. 106.
STRUCTURE-FUNCTION RELATIONSHIPS OF A CATALYTICALLY EFFICIENT BETA-D-XYLOSIDASE -
Jordan, D.B. 2007. Structure-function relationships of a catalytically efficient beta-D-xylosidase [abstract]. American Chemical Society. Paper No. 175.
PRODUCTION OF HIGHLY ACTIVE LIGNOCELLULOSE-DEGRADING ENZYMES OF ANAEROBIC FUNGI BY INDUSTRIALLY RELEVANT FUNGI -
Li, X., Skory, C.D., Ximenes, E.A., Jordan, D.B., Dien, B.S., Hughes, S.R., Cotta, M.A. 2007. Production of highly active lignocellulose-degrading enzymes of anaerobic fungi by industrially relevant fungi [abstract]. Physiology to Genomics to Fuels.
EXPRESSION OF AN AT-RICH XYLANASE GENE FROM THE ANAEROBIC FUNGUS ORPINOMYCES SP. STRAIN PC-2 IN AND SECRETION OF THE HETEROLOGOUS ENZYME BY HYPOCREA JECORINA -
Li, X., Skory, C.D., Ximenes, E.A., Jordan, D.B., Dien, B.S., Hughes, S.R., Cotta, M.A. 2007. Expression of an AT-rich xylanase gene from the anaerobic fungus Orpinomyces sp. strain PC-2 in and secretion of the heterologous enzyme by Hypocrea jecorina. Applied Microbiology and Biotechnology. 74:1264-1275.
FUNGICIDAL CARBOXAMIDES -
Basarab, G.S., Jordan, D.B., Lessen, T.A., Hansen, S.L. 2006. Fungicidal carboxamides. U.S. Patent 7,135,585.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM OF GLYCOSIDE HYDROLASE FAMILY 43 -
Jordan, D.B., Li, X., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. 2007. Beta-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43. Applied Biochemistry and Biotechnology. 136-140:93-104.
HEMICELLULASES FOR MEDIATING BIOMASS SACCHARIFICATION -
HEMICELLULASES FOR MEDIATING BIOMASS SACCHARIFICATION -
Jordan, D.B., Dien, B.S., Li, X., Cotta, M.A. 2006. Hemicellulases for mediating biomass saccharification. In: Proceedings of Renewable Energy 2006, October 9-13, 2006, Makuhari Messe, Chiba, Japan. p. 1036-1041.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM OF GLYCOSIDE HYDROLASE FAMILY 43 -
Jordan, D.B., Li, X., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. 2006. Beta-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43 [abstract]. Gordon Research Conference. p. 3.
STRUCTURE-FUNCTION RELATIONSHIPS OF A CATALYTICALLY EFFICIENT BETA-D-XYLOSIDASE -
Jordan, D.B., Li, X.-L., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. 2007. Structure-function relationships of a catalytically efficient beta-D-xylosidase. Applied Biochemistry and Biotechnology. 141:51-76.
BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM OF GLYCOSIDE HYDROLASE FAMILY 43 -
Jordan, D.B., Li, X., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. 2006. Beta-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43 [abstract]. Biotechnology for Fuels and Chemicals. p.93
CODON OPTIMIZATION OF AN A+T RICH XYLANASE GENE FROM THE ANAEROBIC FUNGUS ORPINOMYCES PC-2 FOR EXPRESSION BY TRICHODERMA REESEI -
Li, X., Jordan, D.B., Ximenes, E.A., Cotta, M.A., Dien, B.S., Hughes, S.R. 2006. Codon optimization of an A+T rich xylanase gene from the anaerobic fungus Orpinomyces PC-2 for expression by Trichoderma reesei [abstract]. In: Proceedings of the 9th International Workshop on Trichoderma and Gliocladium, April 6-8, 2006, Vienna, Austria. Paper No. T3.
ENZYMATIC SACCHARIFICATION OF HOT-WATER PRETREATED CORN FIBER FOR PRODUCTION OF MONOSACCHARIDES -
Dien, B.S., Li, X., Iten, L.B., Jordan, D.B., Nichols, N.N., O Bryan, P.J., Cotta, M.A. 2006. Enzymatic saccharification of hot-water pretreated corn fiber for production of monosaccharides. Enzyme and Microbial Technology. 39:1137-1144.
HETEROLOGOUS PRODUCTION BY TRICHODERMA REESEI OF A XYLANASE OF THE ANAEROBIC FUNGUS ORPINOMYCES PC-2 -
PLASMID-BASED FUNCTIONAL PROTEOMIC ROBOTIC WORKCELL PROCESS FOR HIGH-THROUGHPUT SCREENING OF MULTIPLEXED LIBRARIES OF MUTAGENIZED CLONES -
Hughes, S.R., Riedmuller, S., Mertens, J.A., Li, X., Qureshi, N., Bischoff, K.M., Jordan, D.B., Cotta, M.A., Farrelly, P. 2005. Plasmid-based functional proteomic robotic workcell process for high-throughput screening of multiplexed libraries of mutagenized clones [abstract]. Optimization high-throughput Cultures for Bioprocessing 2005. p. 3.
ACTIVE-SITE MODELS OF RIBOFLAVIN SYNTHASE -
Jordan, D.B., Calabrese, J.C., Liao, D., Wawrzak, Z., Zheng, Y. 2005. Active-site models of riboflavin synthase. In: Nishino, T., Miura, R., Tanokura, M., Fukui, K., editors. Flavins and Flavoproteins 2005. Tokyo: ARchiTect, Inc. p. 737-742.
FUNCTIONAL PROTEOMIC WORKCELL FOR HIGH VOLUME PLASMID PREPARATIONS FOR REPEATED IN VITRO PROTEIN EXPRESSION AND HIGH THROUGHPUT SCREENING TO IDENTIFY MUTANT ENYZMES FOR USE AT LOW PH -
Hughes, S.R., Riedmuller, S.B., Mertens, J.A., Jordan, D.B., Li, X., Qureshi, N., Cotta, M.A., Farrelly, P.J., Bischoff, K.M. 2005. Functional proteomic workcell for high volume plasmid preparations for repeated in vitro protein expression and high throughput screening to identify mutant enyzmes for use at low pH [abstract]. Optimization High-throughput Cultures for Bioprocessing 2005. 13:3.
ENZYMATIC SACCHARIFICATION OF PRETREATED CORN FIBER FOR PRODUCTION OF SUGARS -
Dien, B.S., Li, X., Jordan, D.B., Nichols, N.N., Iten, L.B., Cotta, M.A. 2005. Enzymatic saccharification of pretreated corn fiber for production of sugars [abstract]. International Starch Technology. p. 90.
ACTIVE-SITE MODELS OF RIBOFLAVIN SYNTHASE -
Jordan, D.B., Calabrese, J.C. 2005. Active-site models of riboflavin synthase [abstract]. International Symposium on Flavins and Flavoproteins. p. 104.
SUBSTRATE SPECIFICITIES OF TWO GLYCOSIDE HYDROLASE FAMILY 11 XYLANASES -
Li, X., Jordan, D.B., Cotta, M.A. 2005. Substrate specificities of two glycoside hydrolase family 11 xylanases [abstract]. American Chemical Society. Paper No. 066.
ADVANCES ON ENZYMATIC SACCHARIFICATION OF LIGNOCELLULOSIC BIOMASS -
Li, X., Jordan, D.B., Dien, B.S., Cotta, M.A., Kane, P.M. 2004. Advances on enzymatic saccharification of lignocellulosic biomass [abstract]. Great Lakes Regional American Chemical Society. Paper No. 04-035.
CRYSTAL STRUCTURE OF PHENYLALANINE AMMONIA LYASE: MULTIPLE HELIX DIPOLES IMPLICATED IN CATALYSIS -
Calabrese, J.C., Jordan, D.B., Boodhoo, A., Sariaslani, S., Vannelli, T. 2004. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Journal of Biochemistry. 43:11403-11416.
Last Modified: 5/2/2016
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