Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Towards Sustainable Production of Protein-Rich Foods: Appraisal of Eight Crops for Western Europe. Part II: Analysis of the Technological Aspects of the Production Chain
Swaving Dijkstra, D. ; Linnemann, A.R. ; Boekel, M.A.J.S. van - \ 2003
Critical Reviews in Food Science and Nutrition 43 (2003)5. - ISSN 1040-8398 - p. 481 - 506.
white leaf protein - sodium hexametaphosphate extraction - ammonia-water-treatment - pilot-plant production - rapeseed protein - functional-properties - nutritive-value - toxicological evaluation - chemical-composition - diffusion-extraction
Increased production of plant protein is required to support the production of protein-rich foods which can replace meat in the human diet to reduce the strain that intensive animal husbandry poses on the environment. The suitability of lupin (Lupinus spp.), pea (Pisum sativum), quinoa (Chenopodium quinoa Willd.), triticale (x Triticosecale), lucerne (Medicago sativa), grasses (Lolium and Festuca spp.), rapeseed/canola (Brassica napus) and potato (Solanum tuberosum) for protein production in Western Europe was studied on the basis of a chain-approach. The technological aspects, which are considered in this paper, are the processing methods, and the functional and nutritional properties of the derived protein products. The overall evaluation of the technological prospects of the eight crops as a protein source for Western Europe leads to the conclusion that this part of the production chain is not decisive for that choice. Pea and lupin have a slight advantage over the other crops, because their concentrates and isolates are already commercially available.
Toward Sustainable Production of Protein-Rich Foods: Appraisal of Eight Crops for Western Europe. Part 1. Analysis of the Primary Links of the Production Chain
Linnemann, A.R. ; Swaving Dijkstra, D. - \ 2002
Critical Reviews in Food Science and Nutrition 42 (2002)4. - ISSN 1040-8398 - p. 377 - 401.
quinoa chenopodium-quinoa - alfalfa leaf protein - extruded corn grits - sheep milk cheese - quality characteristics - functional-properties - nutritional quality - sensory evaluation - lupinus-albus - willd seeds
Increased production of plant protein is required to support the production of protein-rich foods that can replace meat in the human diet to reduce the strain that intensive animal husbandry poses to the environment. The suitability of lupin (Lupinusspp.), pea (Pisum sativum), quinoa (Chenopodium quinoaWilld.), triticale (xTriticosecale), lucerne (Medicago sativa), grasses (LoliumandFestucaspp.), rapeseed/canola (Brassica napus), and potato (Solanum tuberosum) for protein production in Western Europe was studied on the basis of a chain approach. The aspects considered are the familiarity of farmers with the cultivation of the crop, prospects for rapid crop improvement, protein production (kg/ha), protein quality (absence of unwanted substances) and familiarity with the usage for human food in Western Europe. Pea, lucerne, and grasses are the most promising, fair prospects are foreseen for lupin, triticale, rapeseed, and potato, whereas the possibilities for quinoa are judged to lag far behind. Estimated protein production for pea, lucerne, and grasses is 1250, 2500, and 2500 kg/ha, respectively
Toward Susti8anable Production of Protein-Rich Foods: Appraisal of Eight Crops For Western Europe. Part1.Analysis of the Primary Links of the Production Chain
Linnemann, A.R. ; Swaving Dijkstra, D. - \ 2002
Critical Reviews in Food Science and Nutrition 42 (2002). - ISSN 1040-8398 - p. 377 - 401.
Towards sustainable production of Protein-Rich Foods
Linnemann, A.R. ; Swaving - Dijkstra, D. ; O'Kane, F. ; Koornneef, M. ; Boekel, M.A.J.S. van; Jongen, W.M.F. - \ 1999
In: Agri-Food Quality II / Hagg, M., Ahvenainen, R., Evers, A.M., Tiiilikala, K., - p. 68 - 70.
Enzymes involved in epoxide degradation in Xanthobacter Py2
Swaving, J. - \ 1998
Agricultural University. Promotor(en): J.A.M. de Bont; A. de Kok. - S.l. : Swaving - ISBN 9789054858560 - 85
microbiële afbraak - microbial degradation
<p>Due to the differences in biological activity of the enantiomers of racemic compounds, the use of enantiomerically pure drugs and agrochemicals is very much encouraged. The availability of optically pure synthons for the production of drugs is, therefor, of the utmost importance for the pharmaceutical industry.</p><p>A very versatile intermediate in organic synthesis is the epoxide group. Epoxides very easily undergo stereospecific ring-opening reactions and are, therefor, very useful to function when available in an enantiomerically pure form as synthons in the production of optically pure drugs.</p><p>In recent years, a great deal of research has been devoted to the development of a biocatalytic method to produces these optically pure epoxides. A very promising method for this is the enantioselective degradation of racemic epoxides (Chapter 2). Although, such a method has a yield of at most 50% it still can be an interesting option, because, racemic epoxides are relatively cheap. A very nice example of enantioselective degradation is found in the bacterium <em>Xanthobacter</em> Py2 which is able to enantioselectively degrade a racemic mixture of 2,3-epoxyalkanes. The 2S-enantiomers are degraded completely, resulting in optically pure 2R-epoxyalkanes.</p><p>At the start of the research done on the degradation of epoxyalkanes by <em>Xanthobacter</em> Py2 described in this thesis, only little information was available on how degradation proceeds. From experiments performed in crude extracts of propene grown <em>Xanthobacter</em> Py2 it was thought that ketones were the product of epoxyalkane degradation (later it was shown epoxyalkanes are carboxylated to<img src="/wda/abstracts/BETA.GIF" ALT="beta" border="0"/>-keto acids). Furthermore, it was concluded that the degradation was dependent on NAD and an unknown low molecular mass compound, which could be replaced by dithiol compounds such as dithiothreitol (DTT).</p><p>To study the degradation of epoxyalkanes by <em>Xanthobacter</em> Py2 in more detail it was decided to do complementation studies using <em>Xanthobacter</em> Py2 mutants devoid of epoxyalkane-degrading activity (Chapter 3). Several cosmids were found complementing restoring the ability of the mutants to grow on epoxides. One of these cosmids, pEP9 was conjugated into <em>Xanthobacter autotrophicus</em> GJ10. This strain is not able to grow on 1,2-epoxypropane nor able to degrade the compound. In crude extracts of <em>Xanthobacter autotrophicus</em> GJ10 complemented with the pEP9, however, epoxyalkane-degrading activity was demonstrated, but only after addition of the LMF or DTT, indicating the right genes were cloned.</p><p>Subcloning revealed a 4.8 kb fragment able to complement the mutation. This fragment was sequenced and found to contain four open reading frames which code for proteins of 41690, 7388, 57315 and 26111 Da, respectively. A homology search using the Swiss-Prot protein bank did reveal little or no homology for the first two ORFs. For ORF4, homologies were found with short-chain alcohol dehydrogenases like 3-oxoacyl reductase and glucose 1-dehydrogenase. Interestingly, ORF3 showed significant homology with pyridine nucleotide-disulfide oxidoreductases like mercury (II) reductase, glutathione reductase and with dihydrolipoamide dehydrogenase.</p><p>In Chapter 4 and Chapter 5, the protein encoded by this third open reading frame was investigated in more detail. All consensus primary structures of pyridine nucleotide-disulfide oxidoreductase are present on the ORF3 amino acid sequence but the C-terminal active site. Furthermore, from the amino acid sequence it was deduced that the nucleotide binding site of NAD(P) showed more resemblance with NADP-dependent proteins then with NAD-dependent proteins, indicating that the ORF3 is NADP-dependent. Using this information the involvement of NADP was tested in the conversion of epoxyalkane in dialyzed crude extracts of propene grown <em>Xanthobacter</em> Py2. It was shown that NADPH and NAD <sup>+</SUP>could restore the epoxyalkane degradation, indicating that NADPH is in fact the low molecular mass fraction. The dithiols replacing the low molecular mass fraction are probably able to directly reduce the redox active disulfide bridge on the ORF3 protein. NADPH also reduces this disulfide bridge by passing on the electrons via a FAD, which is bound to the protein.</p><p>The ORF3 protein was purified and shown to be involved in epoxyalkane degradation by fractionating crude extracts of propene grown <em>Xanthobacter</em> Py2 and complementing fractions without the ORF3 protein with the purified protein, thus restoring the epoxyalkane-degrading activity.</p><p>The purified ORF3 protein in this stage called component II, was characterized (Chapter 5). The protein was shown to be a homodimeric protein, each subunit containing a tightly bound FAD. The spectral properties of the FAD were investigated and kinetic studies were performed to characterize the protein.</p><p>Characterization on component II showed this protein to have common themes as well as distinct difference with other pyridine nucleotide-disulfide oxidoreductases. This comparison gave no clear understanding on the substrate of the component II and its action in the degradation of epoxides.</p><p>Because the component II protein is missing the C-terminal His-Glu dyad active site found in lipoamide dehydrogenases and glutathione reductases, the protein has a very low activity towards dithiols, therefore the substrate of component II may not even be a dithiol compound. 1,2-Epoxypropane is not a substrate for component II, nor is there any interaction with the compound. The involvement of an other (hypothetical) protein, ORF2 ENCODED, is suggested.</p><p>Finally, in Chapter 6, a possible mechanism for 1,2-epoxypropane degradation is discussed.</p>
Microbial transformation of epoxides.
Swaving, J. ; Bont, J.A.M. de - \ 1998
Enzyme and Microbial Technology 22 (1998). - ISSN 0141-0229 - p. 19 - 26.
Enantioselective degradation of racemic epoxides is an interesting method to obtain optically pure epoxides. In this review, an overview is presented on the bioconversion of epoxides in microorganisms. Both the degradation and biosynthesis routes involving epoxides are discussed as well as their usefulness in enantioselective degradation.
Purification and characterization of a flavoprotein involved in the degradation of epoxyalkanes by Xanthobacter Py2.
Westphal, A.H. ; Swaving, J. ; Jacobs, L. ; Kok, A. de - \ 1998
European Journal of Biochemistry 257 (1998). - ISSN 0014-2956 - p. 160 - 168.
A new type of disulfide reductase involved in epoxide degradation by Xanthobacter Py2.
Westphal, A.H. ; Jacobs, L. ; Kok, A. de; Swaving, J. ; Bont, J.A.M. de - \ 1997
In: Flavins and flavoproteins XII / Stevenson, K.J., Massey, V., Williams, C.H., Calgary : University Press - p. 815 - 818.
Dynamic fluorescence spectroscopy on single tryptophan mutants of EIImtl in detergent micelles. Effects of substrate binding and phosphorylation on the fluorescence and anisotropy decay.
Swaving Dijkstra, D. ; Broos, J. ; Visser, A.J.W.G. ; Hoek, A. van; Robillard, G.T. - \ 1997
Biochemistry 36 (1997). - ISSN 0006-2960 - p. 4860 - 4866.
A novel type of pyridine nucleotide disulfide oxireductase is essential for NAD(+) and NADPH-dependent degradation of epoxyalkanes by Xanthobacter strain Py2.
Swaving, J. ; Bont, J.A.M. de; Westphal, A.H. ; Kok, A. de - \ 1996
Journal of Bacteriology 178 (1996). - ISSN 0021-9193 - p. 6644 - 6646.
Electrotransformation of Xanthobacter autotrophicus GJ10 and other Xanthobacter strains.
Swaving, J. ; Leest, W. van; Ooyen, A.J.J. van; Bont, J.A.M. de - \ 1996
Journal of Microbiological Methods 25 (1996). - ISSN 0167-7012 - p. 343 - 348.
Complementation of Xanthobacter Py2 mutants defective in epoxyalkane degradation, and expression and nucleotide sequence of the complementing DNA fragment.
Swaving, J. ; Weijers, C.A.G.M. ; Ooyen, A.J.J. van; Bont, J.A.M. de - \ 1995
Microbiology 141 (1995). - ISSN 1350-0872 - p. 477 - 484.
Sequence of a 4.8 KB DNA fragment complementing a Xanthobacter Py2 mutant defective in epoxyalkane degradation.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1995
In: Abstract 7th European Congr. on Biotechnology. Nice, France. Abstract book 2 (1995) 56 MAP 22
Sequence analysis of a DNA fragment complementing Xanthobacter Py2 mutants defective in epoxyalkane degradation.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1995
BioSpektrum (1995). - ISSN 0947-0867 - p. 79 - PB008.
Complementation of epoxidase negative mutants of Xanthobacter Py2.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1994
In: Abstract 7th Int. Symp. Genetics of industrial microorganisms, Québec, Canada - p. 114 - 114.
Complementation of mutants of Xanthobacter Py2 defective in epoxyalkane degradation.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1994
In: Abstract 5th Neth. Congr. Biotechnology. Amsterdam (1994) PL-12
Initial characterization of the enzyme and cloning of genes involved in the enantioselective epoxyalkane degradation by Xanthobacter Py2.
Swaving, J. ; Weijers, C.A.G.M. ; Chan Kwo Chion, C.K. ; Leak, D.J. ; Ooyen, A.J.J. van; Bont, J.A.M. de - \ 1994
Biocatalysis 10 (1994). - ISSN 0886-4454 - p. 227 - 232.
The genetics of the epoxyalkane degradation in Xanthobacter Py2.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1993
In: Abstract 6th Eur. Congr. Biotechnology, Florence (1993) vol.3, WE166
Cloning of a gene involved in the epoxyalkane degradation in Xanthobacter Py2.
Swaving, J. ; Bont, J.A.M. de; Ooyen, A.J.J. van - \ 1993
In: Abstract 1st Dutch-Japanese Workshop Biocatalysis, Noordwijk (1993) 25. Ook: Eur. Symp. Biocatalysis, Graz, Austria (1993) P-51
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