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|Facilities Planning Promoting Efficient Space Use at Hospital Building
Zijlstra, E. ; Mobach, M.P. ; Schans, C. van der; Hagedoorn, M. - \ 2014
In: Research Papers: Advancing Knowledge in FM : Promoting Innovation in FM. - - p. 366 - 377.
Business opportunities and food safety of the Myanmar edible oil sector
Wijnands, J.H.M. ; Biersteker, J. ; Hagedoorn, L.F. ; Louisse, J. - \ 2014
Wageningen : LEI Wageningen UR (Report / LEI Wageningen UR 2014-036) - ISBN 9789086157013 - 94
oliezaden - spijsoliën - voedselveiligheid - sesamolie - palmoliën - export - bedrijfseconomie - myanmar - oilseeds - edible oils - food safety - sesame oil - palm oils - exports - business economics
This report analyses the business opportunities of the oilseed and edible oil sector in Myanmar as well as the food safety control system. Myanmar is a significant producer of oilseed specialities. It is world’s largest producer of sesame seeds, ranks on the sixth position for groundnut production and for mustard seeds on the third position. However, the exports are insignificant. The food safety control system of this sector is developed weakly. Myanmar has huge opportunities on the world market: foreign currency earnings are in the magnitude of country’s total trade deficit by exporting sesame oil substituted by importing a same amount of palm oil.
The tungsten metallome of Pyrococcus furiosus
Sevcenco, A.M. ; Pinkse, M.W.H. ; Bol, E. ; Krijger, G.C. ; Wolterbeek, H.T. ; Verhaert, P. ; Hagedoorn, P.L. ; Hagen, W.R. - \ 2009
Metallomics 1 (2009)5. - ISSN 1756-5901 - p. 395 - 402.
formaldehyde ferredoxin oxidoreductase - hyperthermophilic archaeon - containing enzyme - chemistry - temperature - protein
The tungsten metallome of the hyperthermophilic archaeon Pyrococcus furiosus has been investigated using electroanalytical metal analysis and native-native 2D-PAGE with the radioactive tungsten isotope W-187 (t(1/2) = 23.9 h). P. furiosus cells have an intracellular tungsten concentration of 29 mu M, of which ca. 30% appears to be free tungsten, probably in the form of tungstate or polytungstates. The remaining 70% is bound by five different tungsten enzymes: formaldehyde ferredoxin oxidoreductase, aldehyde ferredoxin oxidoreductase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase and the tungsten-containing oxidoreductases WOR4 and WOR5. The membrane proteome of P. furiosus is devoid of tungsten. The differential expression, as measured by the tungsten level, of the five soluble tungsten enzymes when the cells are subjected to a cold-shock shows a strong correlation with previously published DNA microarray analyses
In Vivo Performance Testing of the Novel Medspray (R) Wet Aerosol Inhaler
Munnik, P. ; Boer, A.H. de; Wissink, J. ; Hagedoorn, P. ; Heskamp, I. ; Kruijf, W. de; Rijn, C.J.M. van; Frijlink, H.W. ; Zanen, P. - \ 2009
Journal of Aerosol Medicine and Pulmonary Drug Delivery 22 (2009)4. - ISSN 1941-2711 - p. 317 - 321.
optimal particle-size - mild asthmatics - deposition - salbutamol - efficacy - delivery
Background: Monodisperse salbutamol inhalers were compared to select the optimal mass median aerodynamic diameter: 4.0, 5.0 or 6.0 mu m. Methods: Fifteen mild asthmatic patients participated. In all a FEV1-response of >12% (vs. baseline) or >200 mL after inhalation of 200 mu g salbutamol was measured. Each patient was studied four times with intervals of 1 week (three active and one placebo inhaler). First, 10 mu g salbutamol was administered, followed by 10, 20, and 40 mu g, resulting in cumulative doses of 10, 20, 40, and 80 mu g salbutamol. The FEV1 and other lung function parameters were assessed at baseline and 30 min after inhalation of each consecutive dose. Five minutes later a next inhalation was given. Results: The 4.0- and 5.0-mu m droplets did not differ from placebo (p = 0.502, p = 0.127), but the 6.0-mu m droplets differed significantly (p = 0.003). The difference between 6.0-4.0 mu m droplets was significant (p = 0.020), but not between the 6.0-5.0 mu m droplets (p = 0.129). The FEV1 increase after 80-mu g salbutamol for the 6.0-mu m droplets was 243 +/- 144 mL. Conclusions: The study showed that the 6.0-mu m droplets differed from the others in terms of FEV1-improvement, and hence, are the most efficacious of the three evaluated
Purification and characterization of a chlorite dismutase from Pseudomonas chloritidismutans
Mehboob, F. ; Wolterink, A.F.W.M. ; Vermeulen, A.J. ; Jiang, B. ; Hagedoorn, P.L. ; Stams, A.J.M. ; Kengen, S.W.M. - \ 2009
FEMS Microbiology Letters 293 (2009)1. - ISSN 0378-1097 - p. 115 - 121.
desulfovibrio-vulgaris hildenborough - (per)chlorate-reducing bacteria - strain gr-1 - reductase - catalase
The chlorite dismutase (Cld) of Pseudomonas chloritidismutans was purified from the periplasmic fraction in one step by hydroxyapatite chromatography. The enzyme has a molecular mass of 110 kDa and consists of four 31-kDa subunits. Enzyme catalysis followed Michaelis-Menten kinetics, with Vmax and K(m) values of 443 U mg(-1) and 84 microM, respectively. A pyridine-NaOH-dithionite-reduced Cld revealed a Soret peak at 418 nm, indicative for protoheme IX. The spectral data indicate the presence of 1.5 mol protoheme IX mol(-1) tetrameric enzyme while metal analysis revealed 2.2 mol iron mol(-1) tetrameric enzyme. High concentrations of chlorite resulted in the disappearance of the Soret peak, which coincided with loss in activity. Electron paramagnetic resonance analyses showed an axial high-spin ferric iron signal. Cld was inhibited by cyanide, azide, but not by hydroxylamine or 3-amino-1,2,3-triazole. Remarkably, the activity was drastically enhanced by kosmotropic salts, and chaotropic salts decreased the activity, in accordance with the Hofmeister series. Chlorite conversion in the presence of 18O-labeled water did not result in the formation of oxygen with a mass of 34 (16O-18O) or a mass of 36 ((18)O-(18)O), indicating that water is not a substrate in the reaction and that both oxygen atoms originate from chlorite
Two W-containing formate dehydrogenase (CO2 reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans
Bok, F.A.M. de; Hagedoorn, P.L. ; Silva, P.J. ; Hagen, W.R. ; Schiltz, E. ; Fritsche, K. ; Stams, A.J.M. - \ 2003
European Journal of Biochemistry 270 (2003)11. - ISSN 0014-2956 - p. 2476 - 2485.
sulfate-reducing bacterium - desulfovibrio-gigas - oxidizing bacterium - spectroscopic characterization - clostridium-thermoaceticum - phylogenetic analysis - escherichia-coli - pure culture - sp-nov - purification
Two formate dehydrogenases (CO2-reductases) (FDH-1 and FDH-2) were isolated from the syntrophic propionate-oxidizing bacterium Syntrophobacter fumaroxidans. Both enzymes were produced in axenic fumarate-grown cells as well as in cells which were grown syntrophically on propionate with Methanospirillum hungatei as the H2 and formate scavenger. The purified enzymes exhibited extremely high formate-oxidation and CO2-reduction rates, and low Km values for formate. For the enzyme designated FDH-1, a specific formate oxidation rate of 700 U·mg-1 and a Km for formate of 0.04 mm were measured when benzyl viologen was used as an artificial electron acceptor. The enzyme designated FDH-2 oxidized formate with a specific activity of 2700 U·mg-1 and a Km of 0.01 mm for formate with benzyl viologen as electron acceptor. The specific CO2-reduction (to formate) rates measured for FDH-1 and FDH-2, using dithionite-reduced methyl viologen as the electron donor, were 900 U·mg-1 and 89 U·mg-1, respectively. From gel filtration and polyacrylamide gel electrophoresis it was concluded that FDH-1 is composed of three subunits (89 ± 3, 56 ± 2 and 19 ± 1 kDa) and has a native molecular mass of approximately 350 kDa. FDH-2 appeared to be a heterodimer composed of a 92 ± 3 kDa and a 33 ± 2 kDa subunit. Both enzymes contained tungsten and selenium, while molybdenum was not detected. EPR spectroscopy suggested that FDH-1 contains at least four [2Fe-2S] clusters per molecule and additionally paramagnetically coupled [4Fe-4S] clusters. FDH-2 contains at least two [4Fe-4S] clusters per molecule. As both enzymes are produced under all growth conditions tested, but with differences in levels, expression may depend on unknown parameters.
Characterization of the chlorate reductase from Pseudomonas chloritidismutans
Wolterink, A.F.W.M. ; Schiltz, E. ; Hagedoorn, P.L. ; Hagen, W.R. ; Kengen, S.W.M. ; Stams, A.J.M. - \ 2003
Journal of Bacteriology 185 (2003)10. - ISSN 0021-9193 - p. 3210 - 3213.
desulfovibrio-vulgaris hildenborough - nitrate reductase - paracoccus-denitrificans - haloarcula-marismortui - energy transduction - oxide reductase - purification - dehydrogenase - (per)chlorate - enzymes
A chlorate reductase has been purified from the chlorate-reducing strain Pseudomonas chloritidismutans. Comparison with the periplasmic (per)chlorate reductase of strain GR-1 showed that the cytoplasmic chlorate reductase of P. chloritidismutans reduced only chlorate and bromate. Differences were also found in N-terminal sequences, molecular weight, and subunit composition. Metal analysis and electron paramagnetic resonance measurements showed the presence of iron and molybdenum, which are also found in other dissimilatory oxyanion reductases
Audiogram of a striped dolphin (Stenella coeruleoalba)
Kastelein, R.A. ; Hagedoorn, M. ; Au, W.W.L. ; Haan, D. de - \ 2003
Journal of the Acoustical Society of America 113 (2003)2. - ISSN 0001-4966 - p. 1130 - 1137.
The underwater hearing sensitivity of a striped dolphin was measured in a pool using standard psycho-acoustic techniques. The go/no-go response paradigm and up¿down staircase psychometric method were used. Auditory sensitivity was measured by using 12 narrow-band frequency-modulated signals having center frequencies between 0.5 and 160 kHz. The 50 percent detection threshold was determined for each frequency. The resulting audiogram for this animal was U-shaped, with hearing capabilities from 0.5 to 160 kHz (8 1/3 oct). Maximum sensitivity (42 dB re 1 muPa) occurred at 64 kHz. The range of most sensitive hearing (defined as the frequency range with sensitivities within 10 dB of maximum sensitivity) was from 29 to 123 kHz (approximately 2 oct). The animal's hearing became less sensitive below 32 kHz and above 120 kHz. Sensitivity decreased by about 8 dB per octave below 1 kHz and fell sharply at a rate of about 390 dB per octave above 140 kHz
Underwater audiogram of a Pacific walrus (Odobenus rosmarus divergens) measured with narrow-band frequency-modulated signals
Kastelein, R.A. ; Mosterd, P. ; Santen, B. van; Hagedoorn, M. ; Haan, D. de - \ 2002
Journal of the Acoustical Society of America 112 (2002)5. - ISSN 0001-4966 - p. 2173 - 2182.
The underwater hearing sensitivity of an 18-year-old male Pacific walrus was measured in a pool by using a go/no-go response paradigm and the up-down staircase method. Auditory sensitivity was measured using narrow-band, frequency-modulated signals (1500 ms duration) with center frequencies ranging from 0.125 to 15 kHz. The resulting underwater audiogram (50 The range of best hearing (10 dB from the maximum sensitivity) was from 1 to 12 kHz. Sensitivity fell gradually below 1 kHz and dropped off sharply above 12 kHz. The animal showed a peculiar insensitivity for 2 kHz signals. His much higher sensitivity for 1.5- and 3-kHz signals indicated that this is a narrow-band phenomenon. Walrus hearing is relatively sensitive to low frequency sound, thus the species is likely to be susceptible to anthropogenic noise. The thresholds found during a small test with four frequencies with signal durations of 300 ms did not differ significantly from those obtained with signal durations of 1500 ms.
Audiogram of a harbor porpoise (Phocoena phocoena) measured with narrow-band frequency-modulated signals
Kastelein, R.A. ; Bunskoek, P. ; Hagedoorn, M. ; Au, W.W.L. ; Haan, D. de - \ 2002
Journal of the Acoustical Society of America 112 (2002). - ISSN 0001-4966 - p. 334 - 344.
The underwater hearing sensitivity of a two-year-old harbor porpoise was measured in a pool using standard psycho-acoustic techniques. The go/no-go response paradigm and up–down staircase psychometric method were used. Auditory sensitivity was measured by using narrow-band frequency-modulated signals having center frequencies between 250 Hz and 180 kHz. The resulting audiogram was U-shaped with the range of best hearing (defined as 10 dB within maximum sensitivity) from 16 to 140 kHz, with a reduced sensitivity around 64 kHz. Maximum sensitivity (about 33 dB re 1 ?Pa) occurred between 100 and 140 kHz. This maximum sensitivity range corresponds with the peak frequency of echolocation pulses produced by harbor porpoises (120–130 kHz). Sensitivity falls about 10 dB per octave below 16 kHz and falls off sharply above 140 kHz (260 dB per octave). Compared to a previous audiogram of this species (Andersen, 1970), the present audiogram shows less sensitive hearing between 2 and 8 kHz and more sensitive hearing between 16 and 180 kHz. This harbor porpoise has the highest upper-frequency limit of all odontocetes investigated. The time it took for the porpoise to move its head 22 cm after the signal onset (movement time) was also measured. It increased from about 1 s at 10 dB above threshold, to about 1.5 s at threshold.
The Nature of the intermediates in the reactions of Fe(III)- and Mn(III)-microperoxidase-8 with H2O2 : a rapid kinetic study
Primus, J.L. ; Grunenwald, S. ; Hagedoorn, P.L. ; Albrecht-Gary, A.M. ; Mandon, D. ; Veeger, C. - \ 2002
Journal of the American Chemical Society 124 (2002)7. - ISSN 0002-7863 - p. 1214 - 1221.
Kinetic studies were performed with microperoxidase-8 (Fe(III)MP-8), the proteolytic breakdown product of horse heart cytochrome c containing an octapeptide linked to an iron protoporphyrin IX. Mn(III) was substituted for Fe(III) in Mn(III)MP-8.The mechanism of formation of the reactive metal-oxo and metal-hydroperoxo intermediates of M(III)MP-8 upon reaction of H2O2 with Fe(III)MP-8 and Mn(III)MP-8 was investigated by rapid-scan stopped-flow spectroscopy and transient EPR. Two steps (kobs1 and kobs2) were observed and analyzed for the reaction of hydrogen peroxide with both catalysts. The plots of kobs1 as function of [H2O2] at pH 8.0 and pH 9.1 for Fe(III)MP-8, and at pH 10.2 and pH 10.9 for Mn(III)MP-8, exhibit saturation kinetics, which reveal the accumulation of an intermediate. Double reciprocal plots of 1/kobs1 as function of 1/[H2O2] at different pH values reveal a competitive effect of protons in the oxidation of M(III)MP-8. This effect of protons is confirmed by the linear dependence of 1/kobs1 on [H ] showing that kobs1 increases with the pH. The UV-visible spectra of the intermediates formed at the end of the first step (kobs1) exhibit a spectrum characteristic of a high-valent metal-oxo intermediate for both catalysts. Transient EPR of Mn(III)MP-8 incubated with an excess of H2O2, at pH 11.5, shows the detection of a free radical signal at g 2 and of a resonance at g 4 characteristic of a Mn(IV) (S = 3/2) species. On the basis of these results, the following mechanism is proposed: (i) M(III)MP-8-OH2 is deprotonated to M(III)MP-8-OH in a rapid preequilibrium step, with a pKa = 9.2 ± 0.9 for Fe(III)MP-8 and a pKa = 11.2 ± 0.3 for Mn(III)MP-8; (ii) M(III)MP-8-OH reacts with H2O2 to form Compound 0, M(III)MP8-OOH, with a second-order rate constant k1 = (1.3 ± 0.6) x 106 M-1?s-1 for Fe(III)MP-8 and k1 = (1.6 ± 0.9) x 105 M-1?s-1 for Mn(III)MP-8; (iii) this metal-hydroperoxo intermediate is subsequently converted to a high-valent metal-oxo species, M(IV)MP-8=O, with a free radical on the peptide (R ). The first-order rate constants for the cleavage of the hydroperoxo group are k2 = 165 ± 8 s-1 for Fe(III)MP-8 and k2 = 145 ± 7 s-1 for Mn(III)MP-8; and (iv) the proposed M(IV)MP-8=O(R ) intermediate slowly decays (kobs2) with a rate constant of kobs2 = 13.1 ± 1.1 s-1 for Fe(III)MP-8 and kobs2 = 5.2 ± 1.2 s-1 for Mn(III)MP-8. The results show that Compound 0 is formed prior to what is analyzed as a high-valent metal-oxo peptide radical intermediate
Electroanalytical determination of tungsten and molybdenum in proteins
Hagedoorn, P.L. ; Slot, P. van 't; Leeuwen, H.P. van; Hagen, W.R. - \ 2001
Analytical Biochemistry 297 (2001). - ISSN 0003-2697 - p. 71 - 78.
Recent crystal structure determinations accelerated the progress in the biochemistry of tungsten-containing enzymes. In order to characterize these enzymes, a sensitive determination of this metal in protein-containing samples is necessary. An electroanalytical tungsten determination has successfully been adapted to determine the tungsten and molybdenum content in enzymes. The tungsten and molybdenum content can be measured simultaneously from 1 to 10 g of purified protein with little or no sample handling. More crude protein samples require precipitation of interfering surface active material with 10 erchloric acid. This method affords the isolation of novel molybdenum- and tungsten-containing proteins via molybdenum and tungsten monitoring of column fractions, without using radioactive isotopes. A screening of soluble proteins from Pyrococcus furiosus for tungsten, using anion-exchange column chromatography to separate the proteins, has been performed. The three known tungsten-containing enzymes from P. furiosus were recovered with this screening
Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys) (3) ligands
Hagen, W.R. ; Silva, P.J. da; Amorim, M.A. ; Hagedoorn, P.L. ; Wassink, J.H. ; Haaker, H. ; Robb, F.T. - \ 2000
Journal of Biological Inorganic Chemistry 5 (2000). - ISSN 0949-8257 - p. 527 - 534.
Pyrococcus furiosus glyceraldehyde-3-phosphate oxidoreductase has comparable W6+/5+ and W5+/4+ reduction potentials and unusual [4Fe-4S] EPR properties
Hagedoorn, P.L. ; Freije, J.R. ; Hagen, W.R. - \ 1999
FEBS Letters 462 (1999)1. - ISSN 0014-5793 - p. 1 - 2.
|On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus and its putative redox partners: topology, structure, and temperature-dependent redox chemsitry.
Silva, P.J. da; Amorim, M.J. ; Hagedoorn, P.L. ; Wassink, H. ; Haaker, H. ; Hagen, W.R. - \ 1998
In: COST Action 818 Workshop on Bacterial Hydrogenases: Structures and Mechanisms, Sintra, Portugal (1998)
|Hyperthermophilic redox biochemistry revisited: Em(T) profiles of rubredoxin and ferredoxin from Pyrococcus furiosus.
Hagen, W.R. ; Driessen, M.C.P.F. ; Hagedoorn, P.L. ; Bosch, M. van den; Landa, I. ; Arendsen, A.F. ; Silva, P.J. da; Wassink, H. ; Haaker, H. - \ 1998
In: 4th European Biological Inorganic Chemistry Conference, Seville, Spain (1998)
Hyperthermophilic redox chemistry: a re-evaluation.
Hagedoorn, P.L. ; Driessen, M.C.P.F. ; Bosch, M. van den; Landa, I. ; Hagen, W.R. - \ 1998
FEBS Letters 440 (1998). - ISSN 0014-5793 - p. 311 - 314.
Detektie van bodemvocht met X-band SLAR opnamen in een zandgebied
Hagedoorn, F.P. - \ 1989
Wageningen : ICW (ICW nota 1942) - 43
toepassingen - in de grond doordringende radar - kwantitatieve analyse - remote sensing - zandgronden - scannen - grondanalyse - bodemwater - bodemwatergehalte - technieken - microgolfstraling - applications - ground-penetrating radar - quantitative analysis - sandy soils - scanning - soil analysis - soil water - soil water content - techniques - microwave radiation
|Het meten van de reologische eigenschappen van chocolademelk
Hooijdonk, A.C.M. van; Hagedoorn, H.G. ; Vliet, T. van - \ 1984
|De bereiding van drinkyoghurt. 2: De invloed van de produktsamenstelling
Hooijdonk, A.C.M. van; Smalbrink, L. ; Hagedoorn, H.G. ; Reitsma, J.C.E. - \ 1982
Voedingsmiddelentechnologie 15 (1982)20. - ISSN 0042-7934 - p. 25 - 29.