J. A. E. Benen

Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88 (2007)

Pel, H.J., Archer, D.B., Schaap, P.J., Benen, J.A.E., Debets, A.J.M., ...

Fungal polygalacturonase with improved maceration properties (2006)

Benen, J.A.E., Joosten, R., Kars, I., Krooshof, G.H.

A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation (2006)

Martens-Uzunova, E.S., Zandleven, J.S., Benen, J.A.E., Awad, H., Kools, H.J., Beldman, G., ...

The fungus Aspergillus niger is an industrial producer of pectin degrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for...

A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation (2006)

Martens-Uzunova, E.S., Zandleven, J.S., Benen, J.A.E., Awad, H., Kools, H.J., Beldman, G., ...

The fungus Aspergillus niger is an industrial producer of pectindegrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for...

De rol van Botrytis cinerea endopolygalacturonases in pathogenesis: BcPG2 is de belangrijkste virulentie-factor (2006)

Kars, I., Wagemakers, L., Krooshof, G.H., Joosten, R., Benen, J.A.E.

Endopolygalacturonases from Botrytis cinerea: biochemical properties and interaction with inhibiting proteins (2005)

Krooshof, G.H., Joosten, R., Kester, H.C.M., Kars, I., Benen, J.A.E.

The phytopathogen Botrytis cinerea harbours at least six endopolygalacturonase-encoding (Bcpg) genes of which Bcpg1 and Bcpg2 are required for full virulence. The endopolygalacturonase (BcPG) enzymes...

Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris (2005)

Kars, I., Krooshof, G.H., Wagemakers, L., Joosten, R., Benen, J.A.E.

Five Botrytis cinerea endopolygalacturonase enzymes (BcPGs) were individually expressed in Pichia pastoris, purified to homogeneity and biochemically characterized. While the pH optima of the five...

The role of Botrytis cinerea endopolygalacturonases in pathogenesis: BcPG2 is the most important virulence factor (2005)

Kars, I., Wagemakers, L., Krooshof, G.H., Joosten, R., Benen, J.A.E.

Mode of action of xylogalacturonan hydrolase towards xylogalacturonan and xylogalacturonan oligosaccharides (2005)

Zandleven, J.S., Beldman, G., Bosveld, M., Benen, J.A.E., Voragen, A.G.J.

XGH (xylogalacturonan hydrolase; GH 28) is an enzyme that is capable of degrading XGA (xylogalacturonan), which is a polymer of ¿-D-galacturonic acid, highly substituted with ß-D-xylose. XGA is...

Post-translational modifications of recombinant B-cinerea EPG 6 (2005)

Xie, M., Krooshof, G.H., Benen, J.A.E., Atwood, J.A., King, D., Bergmann, C., ...

The fungus Botrytis cinerea is a ubiquitous plant pathogen that infects more than 200 different plant species and causes substantial economic losses in a wide range of agricultural crops and...

Disruption of individual Botrytis cinerea pectinase genes in strain B05.10 showd that Bcpg2, but not Bcpme1, plays a significant role during infection of plants (2004)

Kars, I., Wagemakers, L., Krooshof, G.H., Benen, J.A.E.

Endo-polygalacturonases from Botrytis cinerea: biochemical properties and interaction with inhibiting proteins (2004)

Krooshof, G.H., Joosten, R., Kester, H.C.M., Kars, I., Benen, J.A.E.

Endopolygalacturonases from Botrytis cinerea (2004)

Krooshof, G.H., Joosten, R., Kester, H.C.M., Kars, I., Benen, J.A.E.

Botrytis cinerea endopolygalacturonases possess a strong necrotizing activity (2004)

Kars, I., Krooshof, G.H., Wagemakers, L., Joosten, R., Benen, J.A.E.

The role of Botrytis cinerea endopolygalacturonases during infection (2003)

Kars, I., Krooshof, G.H., Benen, J.A.E.

Characterisation of endopolygalacturonases from Botrytis cinerea (2003)

Krooshof, G.H., Kester, H.C.M., Kars, I., Benen, J.A.E.

Endopolygalacturonases van Botrytris cinerea: karakteristieken in vitro (2003)

Krooshof, G.H., Kester, H.C.M., Burgers, K., Benen, J.A.E.

The role of individual Botrytis cinerea endopolygalacturonases during infection (2003)

Kars, I., Krooshof, G.H., Benen, J.A.E.

Mode of action analysis and structure-function relationships Aspergillus Niger pectinolytic enzymes (2003)

Benen, J.A.E., Voragen, C.H.L., Visser, J.

Pectic Esterases (2003)

Benen, J.A.E., Voragen, A.G.J., Visser, J.

Microbial Pectinases (2003)

Benen, J.A.E., Vincken, J.P.

Pectic enzymes (2003)

Benen, J.A.E., Voragen, A.G.J., Visser, J.

Identification of amino acid residues critical for catalysis and stability in Aspergillus niger family 1 pectin lyase A (2003)

Sanchez-Torres, P., Visser, J., Benen, J.A.E.

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger (2003)

Snijder, H.J., Benen, J.A.E., Dijkstra, B.W.

Polygalacturonases (2003)

Benen, J.A.E., Visser, J.

Pectate and pectin lyases (2003)

Benen, J.A.E., Visser, J.

The contribution of cell wall degrading enzymes to pathogenesis of fungal plant pathogens (2002)

Tenberge, K.B., Benen, J.A.E., Tudzynski, P., Visser, J.

Expression profiling of pectinolytic genes from Aspergillus niger (2002)

Jansen, J., Aguilar, G., Parenicova, L., Joosten, V., Wulfert, F., ...

The expression of 26 pectinolytic genes from Aspergillus niger was studied in a wild type strain and a CreA derepressed strain, under 16 different growth conditions, to obtain an expression profile...

Plant cell wall degrading enzymes produced by Aspergillus (2002)

Benen, J.A.E., Graaff, L.H., Visser, J.

Microbial Pectinases (2002)

Benen, J.A.E., Vincken, J.P.

Use of amide exchange mass spectrometry to study conformational changes within the endopolygalacturonase II-homogalacturonan-polygalacturonase inhibiting protein system (2002)

King, D., Bergmann, C., Orlando, R., Benen, J.A.E., Kester, H.C.M., Visser, J.

Amide exchange mass spectrometry (MS) was used to study the enzyme endopolygalacturonase II (EPG-II) from Aspergillus niger as it binds to an oligosaccharide substrate. A localized decrease in the...

A novel enzyme activity involving de-methylation of specific partially methylated oligogalacturonides (2002)

Williams, M.A.K., Benen, J.A.E.

Studies of the enzymic digestion of pectic substrates using different polygalacturonase (PG) preparations have revealed evidence for a previously unreported enzyme activity carried out by a...

The B1,4- endogalactanase A gene from Aspergillus niger is specifically induced on arabinose and galacturonic acid and plays an important role in the degradation of pectic hairy regions (2002)

Parenicova, L., Hinz, S.W.A., Kester, H.C.M., Benen, J.A.E., Visser, J.

The Aspergillus niger-1,4-endogalactanase encoding gene (galA) was cloned and characterized. The expression of galA in A. niger was only detected in the presence of sugar beet pectin, d-galacturonic...

Microbial pectinases (2002)

Benen, J.A.E., Vincken, J.P.

The ß-1,4-endogalactanase A gene from Aspergillus niger is specifically induced on arabinose and galacturonic acid and plays an important role in the degradation of pectic hairy regions (2002)

Parenicova, L., Hinz, S.W.A., Kester, H.C.M., Beldman, G., Benen, J.A.E., ...

The Aspergillus nigerß-1,4-endogalactanase encoding gene (galA) was cloned and characterized. The expression of galA in A. niger was only detected in the presence of sugar beet pectin,...

Changing a single amino acid residue switches processive and non-processive behavior of Aspergillus niger endopolygalacturonase I and II (2001)

Pages, S., Kester, H.C.M., Visser, J., Benen, J.A.E.

Processivity, also known as multiple attack on a single chain, is a feature commonly encountered only in enzymes in which the substrate binds in a tunnel. However, of the seven Aspergillus niger...

Plant cell wall degrading enzymes produced by Aspergillus (2001)

Benen, J.A.E., Visser, J.

Characterization of pectate lyase A from Aspergillus niger (2001)

Benen, J.A.E., Parenicova, L., Kester, H.C.M., Visser, J.

The Aspergillus niger plyA gene encoding pectate lyase A (EC 4.2.99.3) was cloned from a chromosomal EMBL4 library using the Aspergillus nidulans pectate lyase encoding gene [Dean, R. A., and...

The active-site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis (2000)

Armand, S., Wagemaker, M.J.M., Sanchez-Torres, P., Kester, H.C.M., Dijkstra, B.W., ...

Strictly conserved charged residues among polygalacturonases (Asp-180, Asp-201, Asp-202, His-223, Arg-256, and Lys-258) were subjected to site-directed mutagenesis in Aspergillus niger...

Structure and function of pectic enzymes : Virulence factors of plant pathogens (2000)

Herron, S.R., Benen, J.A.E., Scavetta, R.D., Visser, J., Jurnak, F.

Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase: mode of action on fully methylesterified oligogalacturonates (2000)

Kester, H.C.M., Esteban Warren, M., Orlando, R., Benen, J.A.E., Bergmann, C., Visser, J.

The substrate specificity and the mode of action of Aspergillus niger pectin methylesterase (PME) was determined using both fully methyl-esterified oligogalacturonates with degrees of polymerization...

Subsite Mapping of Aspergillus niger Endopolygalacturonase II by Site-directed Mutagenesis (2000)

Pages, S., Heijne, W.H.M., Kester, H.C.M., Visser, J., Benen, J.A.E.

To assess the subsites involved in substrate binding in Aspergillus niger endopolygalacturonase II, residues located in the potential substrate binding cleft stretching along the enzyme from the N to...

pgaD encodes a new type of endopolygalacturonase from Aspergillus niger (2000)

Parenicova, L., Kester, H.C.M., Benen, J.A.E., Visser, J.

We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A. niger PGs by a 136 amino...

pgaA and pgaB encode constitutively expressed members of the Aspergillus niger endopolygalacturonase gene family (2000)

Parenicova, L., Benen, J.A.E., Kester, H.C.M., Visser, J.

The nucleotide sequence data for pgaA and pgaB have been deposited with the EMBL, GenBank and DDBJ Databases under accession numbers Y18804 and Y18805 respectively. pgaA and pgaB, two genes encoding...

Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I, II and C (1999)

Benen, J.A.E., Kester, H.C.M., Visser, J.

Structure-function relationships in polygalacturonases : a site-directed mutagenesis approach (1999)

Benen, J.A.E., Kester, H.C.M., Armand, S., Sanchez-Torres, P., Parenicová, L., Pagés, S., ...

Flavoprotein kinetics (1999)

Benen, J.A.E., Eppink, M.H.M., Fraaije, M.W.

Characterization of the glycosylation of recombinant endopolygalacturonase I from Aspergillus niger (1999)

Colangelo, J., Licon, V., Benen, J.A.E., Visser, J., Bergmann, C., Orlando, R.

Characterization of the N-linked glycosylation site of recombinant pectate lyase (1999)

Colangelo, J., Licon, V., Benen, J.A.E., Visser, J., Bergmann, C., Orlando, R.

Recombinant pectate lyase from Aspergillus niger was overexpressed in Aspergillus nidulans. The two recombinant proteins produced differed in molecular mass by 1200 Da, which suggested that the...

Performance of selected microbial pectinases on synthetic mono-methylesterified di- and trigalacturonates (1999)

Kester, H.C.M., Magaud, D., Roy, C., Anker, D., Doutheau, A., Shevchik, V., ...

Two monomethyl esters of -(1-4)-linked D-galacturonic dimers and three monomethyl esters of -(1-4)-linked D-galacturonic acid trimers were synthesized chemically and further used as substrates in...

The exopolygalacturonase from Aspergillus tubingensis is also active on xylogalacturonan (1999)

Kester, H.C.M., Benen, J.A.E., Visser, J.

Modes of action of five different endopectate lyases from Erwinia chrystanthemi (1999)

Roy, C., Kester, H.C.M., Visser, J., Shevchik, V.E., Robert-Baudouy, J., ...

Mode of action of five different endopectate lyases from Erwinia chrysanthemi 3937 (1999)

Roy, C., Kester, H.C.M., Benen, J.A.E., Schevchik, V.E., Robert-Baudouy, J., ...

1.68-C Crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis (1999)

Benen, J.A.E., Schroter, K.H., Kalk, K.H., Armand, S., Visser, J., ...

Structure of plant cell wall fragment complexed to pectate lyase C (1999)

Scavetta, R.D., Herron, S.R., Hotchkiss, A.T., Kita, N., Keen, N.T., Benen, J.A.E., ...

Cloning, sequencing and expression of Penicillium simplicissimum cDNA encoding the covalent flavoprotein vanillyl-alcohol oxidase. (1998)

Benen, J.A.E., Wagemaker, M.J.M., Fraaije, M.W., Sanchez-Torres, P., Visser, J.

A novel oxidoreductase family sharing a conserved FAD binding domain. (1998)

Fraaije, M.W., Benen, J.A.E., Visser, J., Mattevi, A.

EU-Project Report: picking out the perfect pectinase. (1998)

Benen, J.A.E., Visser, J.

Rhamnogalacturonases and polygalacturonases of Aspergillus niger. (1998)

Benen, J.A.E., Kester, H.C.M., Parenicova, L., Visser, J.

Molecular cloning, sequencing and heterologous expression of the vaoA gene from Penicillium simplicissimum CBS 170.90 encoding vanillyl-alcohol oxidase. (1998)

Benen, J.A.E., Sanchez-Torres, P., Wagemaker, M.J.M., Fraaije, M.W., Visser, J.

pgaE encodes a fourth member of the endopolygalacturonase gene family from Aspergillus niger. (1998)

Parenicov, L., Benen, J.A.E., Kester, H.C.M., Visser, J.

Structure and mechanism of vanillyl-alcohol oxidase from Penicillium simplicissimum. (1997)

Fraaije, M.W., Benen, J.A.E., Visser, J., Mattevi, A.

Crystal structure of pectin lyase A from Aspergillus niger. (1997)

Mayans, O., Connerton, I., Gravesen, T., Benen, J.A.E., Visser, J., Pickersgill, R., ...

Evaluation of RFLP analysis for the classification of selected black Aspergilli. (1997)

Parenicova, L., Benen, J.A.E., Samson, R.A., Visser, J.

Kinetics and mode of action of Aspergillus niger polygalacturonases. (1996)

Benen, J.A.E., Kester, H.C.M., Parenicová, L., Visser, J.

pgaE from Aspergillus niger encodes a fourth polygalacturonase. Molecular cloning and biochemical characterization of the gene product. (1996)

Parenicová, L., Benen, J.A.E., Kester, H.C.M., Visser, J.

Stereochemistry of hydrolysis of glycosidic linkage by three Aspergillus polygalacturonases. (1996)

Biely, P., Benen, J.A.E., Kester, H.C.M., Heinrichova, K., Visser, J.

Molecular genetic and biochemical aspects of pectin degradation in Aspergillus. (1996)

Benen, J.A.E., Parenicová, L., Kester, H.C.M., Visser, J.

Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme (1996)

Steinebach, V., Benen, J.A.E., Bader, R., Postma, P.W., Vries, S. De, Duine, J.A.

Isolation and characterisation of the pyruvate dehydrogenase complex of anaerobically grown Enterococcus faecalis NCTC 775. (1992)

Snoep, J.L., Westphal, A.H., Benen, J.A.E., Teixeira De Mattos, M.J., Neijssel, O.M.

Lipoamide dehydrogenase from Azotobacter vinelandii: site directed mutagenesis of the his450-glu455 diad. Kinetic properties of wild type and mutated enzymes. (1992)

Benen, J.A.E., Williams, C.H., Arscott, D., Veeger, C.

Lipoamide dehydrogenase from Azotobacter vinelandii: role of C-terminal residues in catalysis and dimer stabilization. (1992)

Benen, J.A.E., Veeger, C.

Studies on lipoamide dehydrogenase. (1992)

Benen, J.A.E.

http://library.wur.nl/wda/abstracts/ab1497.html

Conformational dynamics and intersubunit energy transfer in wild-type and mutant lipoamide dehydrogenase from Azotobacter vinelandii. A multidimensional time-resolved polarized fluorescence study. (1992)

Bastiaens, P.I.H., Benen, J.A.E., Brochon, J.C.

Binding studies of the dihydrolipoamide dehydrogenase component (E3) in the pyruvate dehydrogenase complex from Azotobacter vinelandii. (1991)

Schulze, E., Benen, J.A.E., Westphal, A.H.

Lipoamide dehydrogenase from Azotobacter vinelandii-kinetic studies on wild-type and mutant enzymes. (1991)

Benen, J.A.E.

Site-directed mutagenesis studies on lipoamide dehydrogenase from Azotobacter vinelandii. (1991)

Benen, J.A.E.

Interaction of lipoamide dehydrogenase with the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. (1991)

Schulze, E., Benen, J.A.E., Westphal, A.H.

Lipoamide dehydrogenase from Azotobacter vinelandii: site directed mutagenesis of the his450-glu455 diad. Spectral properties of wild type and mutated enzymes. (1991)

Benen, J.A.E., Zak, Z., Veeger, C.

On the FAD-induced dimerization of apo lipoamide dehydrogenase from Azotobacter vinelandii and Pseudomonas fluorescens (Kinetics of reconstitution). (1991)

Benen, J.A.E., Snoek, M.C.

Site-directed mutagenesis of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. (1991)

Westphal, A.H., Eschrich, K., Benen, J.A.E.

Molecular cloning and sequence determination of the LPD-gene encoding lipoamide dehydrogenase from Pseudomonas fluorescens. (1989)

Benen, J.A.E., Müller, F.

Molecular cloning, purification and some properties of lipoamide dehydrogenase from Pseudomonas fluorescens. (1987)

Benen, J.A.E., Keukens, E.