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.

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Membrane bioreactors for groundwater treatment
Hage, J.C. ; Tramper, J. ; Hartmans, S. - \ 2006
NPT Procestechnologie 13 (2006)1. - ISSN 1380-3638 - p. 9 - 11.
Membrane-aerated biofilm reactor for the removal of 1,2-dichloroethane by Pseudomonas sp strain DCA1
Hage, J.C. ; Houten, R.T. ; Tramper, J. ; Hartmans, S. - \ 2004
Applied Microbiology and Biotechnology 64 (2004)5. - ISSN 0175-7598 - p. 718 - 725.
biologische behandeling - membranen - ethyleendichloride - biofilms - biodegradatie - verwijdering - afvalwaterbehandeling - pseudomonas - insecticiden - beluchting - biological treatment - membranes - ethylene dichloride - biodegradation - removal - waste water treatment - insecticides - aeration - waste-gas treatment - aliphatic-compounds - aerobic biofilms - degradation - groundwater - bioreactor - kinetics - trichloroethylene - model - water
A membrane-aerated biofilm reactor (MBR) with a biofilm of Pseudomonas sp. strain DCA1 was studied for the removal of 1,2-dichloroethane (DCA) from water. A hydrophobic membrane was used to create a barrier between the liquid and the gas phase. Inoculation of the MBR with cells of strain DCA1 grown in a continuous culture resulted in the formation of a stable and active DCA-degrading biofilm on the membrane. The maximum removal rate of the MBR was reached at a DCA concentration of approximately 80 µM. Simulation of the DCA fluxes into the biofilm showed that the MBR performance at lower concentrations was limited by the DCA diffusion rate rather than by kinetic constraints of strain DCA1. Aerobic biodegradation of DCA present in anoxic water could be achieved by supplying oxygen solely from the gas phase to the biofilm grown on the liquid side of the membrane. As a result, direct aeration of the water, which leads to undesired coagulation of iron oxides, could be avoided
A membrane-aerated biofilm reactor (MBR) with a biofilm of Pseudomonas sp. strain DCA1 was studied for the removal of 1,2-dichloroethane (DCA) from water. A hydrophobic membrane was used to create a barrier between the liquid and the gas phase. Inoculation of the MBR with cells of strain DCA1 grown in a continuous culture resulted in the formation of a stable and active DCA-degrading biofilm on the membrane. The maximum removal rate of the MBR was reached at a DCA concentration of approximately 80 muM. Simulation of the DCA fluxes into the biofilm showed that the MBR performance at lower concentrations was limited by the DCA diffusion rate rather than by kinetic constraints of strain DCA1. Aerobic biodegradation of DCA present in anoxic water could be achieved by supplying oxygen solely from the gas phase to the biofilm grown on the liquid side of the membrane. As a result, direct aeration of the water, which leads to undesired coagulation of iron oxides, could be avoided.
Application of Pseudomonas sp. strain DCA1 for the removal of chlorinated hydrocarbons
Hage, J.C. - \ 2004
Wageningen University. Promotor(en): Hans Tramper, co-promotor(en): S. Hartmans. - [S.l.] : S.n. - ISBN 9085040795 - 126
oplosmiddelverwijdering - gechloreerde koolwaterstoffen - biofilms - bioreactoren - microbiële afbraak - pseudomonas - membranen - solvent removal - chlorinated hydrocarbons - biofilms - bioreactors - microbial degradation - pseudomonas - membranes
Enzymatic synthesis of thioglucosides using almond ß-glucosidase
Meulenbeld, G.H. ; Roode, B.M. de; Hartmans, S. - \ 2002
Biocatalysis and Biotransformation 20 (2002)4. - ISSN 1024-2422 - p. 251 - 256.
A selection of different glycosidases was screened for the glycosylation of 1-propanethiol. The g-glucosidases from almond, Aspergillus niger and Caldocellum saccharolyticum were capable of 1-propanethioglucoside (1-PTG) formation. The almond g-glucosidase showed the highest activity in this reversed hydrolysis type of reaction using glucose as glucosyl donor. Besides 1-propanethiol, also thioglucosides of 2-propanethiol and furfuryl mercaptan were formed by the almond g-glucosidase. The substrate specificity of the almond g-glucosidase with respect to thioglucosylation is restricted to primary and secondary aliphatic thiols. Once the thioglucosides are formed, they are not hydrolyzed at a significant rate by almond g-glucosidase. As a consequence the synthesis of 1-PTG could be observed at very low aglycone concentrations (0.5␟/v based on the reaction solution) and high yields (68␋ased on 1-PT and 41␋ased on glucose) were obtained. An excess of aglycone, otherwise frequently applied in reversed hydrolysis glycosylation, is therefore not necessary in the glucosylation of 1-PT.
Concominant extracellular accumulation of alpha-keto acids and higher alcohols by Zygosaccharomyces rouxii
Sluis, C. van der; Rahardjo, Y.S.P. ; Smit, B.A. ; Kroon, P.J. ; Hartmans, S. ; Schure, E.G. ter; Tramper, J. ; Wijffels, R.H. - \ 2002
Journal of Bioscience and Bioengineering 93 (2002). - ISSN 1389-1723 - p. 117 - 124.
Alpha-keto acids are key intermediates in the formation of higher alcohols, important flavor components in soy sauce, and produced by the salt-tolerant yeast Zygosaccharomyces rouxii. Unlike most of the higher alcohols, the alpha-keto acids are usually not extracellularly accumulated by Z. rouxii when it is cultivated with ammonium as the sole nitrogen source. To facilitate extracellular accumulation of the alpha-keto acids from aspartate-derived amino acid metabolism, the amino acids valine, leucine, threonine and methionine were exogenously supplied during batch and A-stat cultivations of (mutants of) Z. rouxii. It was shown that all alpha-keto acids from the aspartate-derived amino acid metabolism, except alpha-ketobutyrate, could be extracellularly accumulated. In addition, it appeared from the concomitant extracellular accumulation of alpha-keto acids and higher alcohols that in Z. rouxii, valine, leucine and methionine were converted via Ehrlich pathways similar to those in Saccharomyces cerevisiae. Unlike these amino acids, threonine was converted via both the Ehrlich and amino acid biosynthetic pathways in Z. rouxii.
Klaasje J. Hartmans : investeren in onderzoek naar plantaardige bestrijdingsmiddelen noodzakelijk
Delft, R. van - \ 2001
Aardappelwereld 55 (2001)4. - ISSN 0169-653X - p. 4 - 5.
aardappelen - investering - opslag - behoud - bestraling - pesticiden - gewasbescherming - wetgeving - agrarisch recht - nederland - europa - onderzoek - recht - potatoes - storage - preservation - irradiation - pesticides - plant protection - investment - legislation - agricultural law - research - netherlands - europe - law
Bij het zoeken naar een alternatief voor kiemremmingsmiddelen voor de aardappel ontdekte men de plantaardige stof carvon als goede vervanger. De regelgeving in Nederland en binnen Europa is dermate dichtgetimmerd, dat zelfs het onderzoek naar toepassing van dit middel, dat gewonnen kan worden uit Karwijzaad, geldverslindend wordt
Co-metabolic degradation of chlorinated hydrocarbons by Pseudomonas sp. strain DCA1
Hage, J.C. ; Kiestra, F.D.G. ; Hartmans, S. - \ 2001
Applied Microbiology and Biotechnology 57 (2001). - ISSN 0175-7598 - p. 548 - 554.
Thioglucosidase activity from Sphingobacterium sp. strain OTG1
Meulenbeld, G.H. ; Hartmans, S. - \ 2001
Applied Microbiology and Biotechnology 56 (2001). - ISSN 0175-7598 - p. 700 - 706.
Screening for novel thioglucoside hydrolase activity resulted in the isolation of Sphingobacterium sp. strain OTG1 from enrichment cultures containing octylthioglucoside (OTG). OTG was hydrolysed into octanethiol and glucose by cell free extracts. Besides thioglucoside hydrolysis, several other glucoside hydrolase activities were detected in the Sphingobacterium sp. strain OTG1 cell free extract. By adding β-glucosidase inhibitors it was possible to discriminate between these different activities. Ascorbic acid and D-gluconic acid lactone inhibited the hydrolysis of p-nitrophenyl β-glucoside, but did not affect octyl- and octylthioglucoside hydrolase activity. Besides OTG, various other thioglucosides were hydrolysed by the novel thioglucosidase, with almost the same activities regardless of the nature of the aglycone, including the myrosinase model substrate sinigrin (a glucosinolate). Sinigrin could also be used as a growth substrate by Sphingobacterium sp. strain OTG1, although at concentrations exceeding 0.15 mM degradation was not complete.
Enzymatic glucosylation: sucrose glucosyltransferases and glucosidases in O- and S-glucoside synthesis
Meulenbeld, G.H. - \ 2001
Wageningen University. Promotor(en): A.G.J. Voragen; S. Hartmans. - S.l. : S.n. - ISBN 9789058085269 - 112
sucrose - glucose - catechine - glycosyltransferasen - sucrose - glucose - catechin - glycosyltransferases

Glycosylation is considered as a useful method for improving chemical properties like solubility and volatility of compounds with interesting organoleptic or physiological properties. The aim of the research described in this thesis was to explore the enzymatic glycosylation of aglycones (nonsaccharide acceptor molecules). The initial focus is on the glucosylation of aromatic alcohols by non-Leloir glucosyltransferases like sucrose glucosyltransferases.
Several streptococcal sucrose glucosyltransferases (glucansucrases) were screened for transglucosylation activity using the flavonoid catechin as model aglycone and sucrose as an economically feasible glucosyl donor substrate (Chapter 2). Streptococcusmutans GS-5 glucosyltransferase-D (GTF-D) glucosylated catechin most efficiently (90% catechin yield). Three different catechin glucosides were isolated of which two catechin glucoside structures were spectroscopically elucidated; catechin-4'- O -α-D- and catechin-4',7- O -α-di-D-glucopyranoside. The structure of the third glucoside remained unsolved, although hydrolysis studies using Aspergillusniger amyloglucosidase suggested that catechin-7- O -α-D-glucopyranoside was formed. The acceptor specificity of GTF-D towards aromatic aglycones is restricted to compounds containing two adjacent aromatic hydroxyl groups, e.g. (substituted) catechol(s) (Chapter 3). This suggests that one hydroxyl group is involved in the interaction with GTF-D, while the other is available for formation of the glucosidic linkage. Compounds containing one hydroxyl group like phenol, irreversibly inhibit GTF-D transglucosylation activity.
To facilitate the transglucosylation of less water soluble aglycones, the addition of water miscible organic solvents (cosolvents) was studied (Chapter 3). Bis-2-methoxyethyl ether (MEE) was selected as the most appropriate cosolvent. MEE addition resulted in a 4-fold increase in catechin transglucosylation activity due to a 12-fold increase in catechin solubility. Addition of MEE (10-30% v/v) also enabled the glucosylation of catechol aglycones at otherwise inhibitory concentrations (200 mM). This was explained by assuming that the partitioning of the aglycone between solvent and enzyme was changed upon MEE addition.
The addition of bis-2-methoxyethyl ether also affected the formation rate and absolute amounts of glucan formed (Chapter 4). An increase of 20% in reducing sugars was observed using 20% (v/v) MEE. Besides an increase in sucrose hydrolysis there was also an increase the formation of high molecular weight glucan chains (10 2-10 3kDa). Linkage analysis showed that also the type of glucosidic linkage was affected upon MEE addition. Glucan formed in the presence of MEE contained an increased amount ofα(1,3) linkages. It was hypothesised that MEE affected glucan formation through modifying the GTF-D glucan binding domain.
The accumulation of fructose was shown to inhibit aglycon glucosylation and glucan formation. To overcome this inhibition, the fructose consuming yeasts Pichiapastoris and the mutant Saccharomycescerevisiae T2-3D were added (Chapter 2). Both yeasts are incapable of utilising sucrose. Due to the consumption of fructose during transglucosylation, an increase in glucoside yield and the maximum duration of catechin glucosylation was observed. Consequently, the consumption of sucrose by GTF-D increased. Eventually glucosylation yields by GTF-D could be engineered either by adding MEE or by fructose consuming yeasts (Chapter 2 and 3). Using MEE, the glucoside yield based on catechin decreased and the sucrose based yield increase. The addition of the yeasts resulted in an increased catechin based glucoside yield and a decreased sucrose based glucoside yield.
In the second part of this thesis the attention is focussed on glycosidases and the hydrolysis and formation of thioglucosides. The observed stability of thioglucosides towards enzymatic hydrolysis was used to screen for new thioglucoside active enzymes (Chapter 5). Using octylthioglucoside (OTG) as a carbon source for microbial growth, Sphingobacterium sp. strain OTG1 was isolated. In the cell free extract a novel thioglucoside hydrolase activity was observed, showing distinct characteristics compared to typicalβ- or thioglucosidases. Various thioglucosides were hydrolysed by the Sphingobacterium cell free extract, with almost the same activities.
In view of the aim of this thesis, the synthesis of glycosides, various glycosidases were screened for the glycosylation of 1-propanethiol (Chapter 6). Theβ-glucosidase from almond, Aspergillusniger and Caldocellumsaccharolyticum showed thioglucosylation activity using glucose and 1-propanetiol. The almond enzyme showed the highest activity (3μmol.min -1.mg -1). Only primary and secondary (10-fold slower reaction rate) aliphatic thiols were glucosylated. Of the different thiols examined, the glucosylation of furfuryl mercaptan is the most interesting because of the potential of the glucoside as a flavour precursor.
Because of the stability of thioglucosides towards most enzymatic hydrolases (glycosidases), an excess of aglycone otherwise frequently applied in reversed hydrolysis glycosylation is not necessary for thioglucosylation. Consequently, high yields up to 60% based on 1-propanethiol and 40% based on glucose were obtained for the synthesis of 1-propanethioglucoside.

Enzymatic modification of bacterial exopolysaccharides : xanthan lyase as a tool for structural and functional modification of xanthan
Ruijssenaars, H.J. - \ 2001
Wageningen University. Promotor(en): J.A.M. de Bont; S. Hartmans. - S.l. : S.n. - ISBN 9789058083739 - 95
polysacchariden - xanthan - lyasen - biodegradatie - polysaccharides - xanthan - lyases - biodegradation

Bacterial extracellular polysaccharides (EPSs) can be applied, e.g., in foods, as a thickener or stabilizer. The functional properties that make a polysaccharide suitable for such applications are largely determined by the primary structure, i.e., the sugar composition, the linkage types between the sugar units, and the presence of side chains and non-sugar substituents. The aim of this research was to obtain EPS-modifying enzymes that could be used as tools both for studying structure-function relationships of (food-grade) EPSs and for the production of tailor-made EPSs with a specific, desired functionality. EPS-degrading microorganisms could serve as a source of such enzymes.

To get an idea of the probability of finding EPS-degrading microorganisms, a comparative biodegradability study was carried out on eight EPSs, six of which were produced by lactic acid bacteria (Chapter 2). Human faeces or soil were used as inocula. Xanthan, clavan, and the EPSs of Streptococcus thermophilus strains SFi39 and SFi12 were readily degraded. The four other EPSs, produced by Lactococcus lactis ssp. cremoris B40, Lactobacillus sakei 0-1, S. thermophilus SFi20, and Lactobacillus helveticus Lh59, were not. Xanthan, the most relevant food-grade EPS, was chosen as the target for further studies.

For efficient screening of polysaccharide-degrading microorganisms, plate methods are required that discriminate between intact and degraded polysaccharide. Such methods can make use of specific physicochemical properties of the polysaccharide, such as complex formation with dyes and gelling capacity. Alternatively, dye-labelled polysaccharides can be applied. Chapter 3 presents a survey of plate methods based on the above principles.

A mixed xanthan-degrading culture was obtained from soil by enrichment on xanthan. From this culture, Paenibacillus alginolyticus XL-1 was isolated. This strain degraded 28% of the xanthan molecule and appeared to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including a xanthan lyase. Xanthan lyase removes the terminal mannosyl residue of the trisaccharide xanthan side chain by aβ-eliminative mechanism, resulting in a double bond in the side chain glucuronyl residue. Xanthan lyase is the only polysaccharide lyase that is exo-acting, releasing residues from the outside of a polysaccharide molecule. All other polysaccharide lyases described to date are endo-acting, attacking the polysaccharide backbone. In P. alginolyticus XL-1, xanthan lyase production is induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation products from xanthan. A 97-kDa xanthan lyase was purified and characterized. The enzyme is specific for pyruvated mannosyl side chain residues and optimally active at pH 6.0 and 55°C (Chapter 4).

The gene encoding the pyruvated mannose-specific xanthan lyase of P . alginolyticus XL-1, designated xalA , was isolated. The xalA gene encodes a 936-amino acid protein, including a 36-amino acid signal sequence. The XalA protein belongs to polysaccharide lyase family 8, which until now only contained chondroitinases and hyaluronate lyases. The part of the xalA gene encoding the 900-amino acid, 96,887-Da mature enzyme was expressed functionally in Escherichia coli . Like the native enzyme, the recombinant enzyme is specific for pyruvated xanthan. Heterologous production of XalA in E. coli increased the volumetric productivity by a factor 30, compared to production by P. alginolyticus . The recombinant xanthan lyase was used as a tool to modify xanthan, which resulted in a dramatic loss of the capacity to form gels with locust bean gum.

Besides xanthan lyase, P. alginolyticus XL-1 produces other enzymes that could be useful for xanthan modification, such as a xanthan deacetylase and an enzyme releasing uronic acid, or uronic acid-containing oligosaccharides, from xanthan lyase-modified xanthan. Since these enzymes were produced at very low titers, P. alginolyticus XL-1 is not a suitable production organism for xanthan-modifying enzymes. Strain XL-1 may be very useful, however, as a source of genes for heterologous production of xanthan-modifying enzymes.

Plate screening methods for the detection of polysaccharase-producing microorganisms
Ruijssenaars, H.J. ; Hartmans, S. - \ 2001
Applied Microbiology and Biotechnology 55 (2001)2. - ISSN 0175-7598
Polysaccharide-degrading enzymes (polysaccharases) are widely applied in industry. One of the sources of these enzymes are polysaccharide-degrading microorganisms. To obtain such microorganisms from enrichment cultures, strain collections or gene libraries, efficient plate screening methods are required that discriminate between intact and degraded polysaccharide. This can be achieved by making use of specific physicochemical properties of the polysaccharide, such as complex formation with dyes and gelling capacity, or by the application of dye-labelled polysaccharides. This review presents a survey of plate methods based on these principles. Both theoretical and practical aspects of the methods are discussed.
Use of Life Cycle Assessment in development processes illustrated with a manure treatment system
Satter, I.H.G. ; Starmans, D.A.J. ; Willers, H.C. ; Ogink, N.W.M. ; Groot Koerkamp, P.W.G. - \ 2000
In: Proceedings of the 4th International Symposium on Biotechnology, Noordwijkerhout (NL), 10-12 April / Hartmans, S., Lens, P., - p. 157 - 160.
Performance of a thermophilic sulfate and sulfite reducing high-rate anaerobic reactor fed with methanol
Weijma, J. ; Hulshoff Pol, L.W. ; Stams, A.J.M. ; Lettinga, G. - \ 2000
In: ISEB 4 Proceedings of the 4th International Symposium on Environmental Biotechnology, Noordwijkerhout, 10-12 April 2000 / Hartmans, S., Lens, P.N.L., - p. 222 - 225.
Rates of ammonia assimilation and ammonification during composting - development of methodology
Veeken, A.H.M. ; Hanajima, D. ; Hamelers, H.V.M. - \ 2000
In: ISEB 4 Proceedings of the 4th International Symposium on Environmental Biotechnology, Noordwijkerhout, 10-12 April 2000 / Hartmans, S., Lens, P.N.L., - p. 524 - 527.
Application of redox mediators to accelerate the transformation of reactive azo dyes in anaerobic bioreactors
Zee, F.P. van der; Bouwman, R.H.M. ; Strik, D.P.B.T.B. ; Lettinga, G. ; Field, J.A. - \ 2000
In: ISEB 4 Proceedings of the 4th International Symposium on Environmental Biotechnology, Noordwijkerhout, 10-12 April 2000 / Hartmans, S., Lens, P.N.L., - p. 34 - 37.
Regulation of aspartate-derived amino-acid metabolism in Zygosaccharomyces rouxii compared to Saccharomyces cerevisiae
Sluis, C. van der; Smit, B.A. ; Hartmans, S. ; Schure, E.G. ter; Tramper, J. ; Wijffels, R.H. - \ 2000
Enzyme and Microbial Technology 27 (2000). - ISSN 0141-0229 - p. 151 - 156.
To elucidate the growth inhibitory effect of threonine, the regulation of the aspartate-derived amino-acid metabolism in Zygosaccharomyces rouxii, an important yeast for the flavor development in soy sauce, was investigated. It was shown that threonine inhibited the growth of Z. rouxii by blocking the methionine synthesis. It seemed that threonine blocked this synthesis by inhibiting the conversion of aspartate. In addition, it was shown that the growth of Z. rouxii, unlike that of Saccharomyces cerevisiae, was not inhibited by the herbicide sulfometuron methyl (SMM). From enzyme assays, it was concluded that the acetohydroxy acid synthase in Z. rouxii, unlike that in S. cerevisiae, was not sensitive to SMM. Furthermore, the enzyme assays demonstrated that the activity of threonine deaminase in Z. rouxii, like in S. cerevisiae, was strongly inhibited by isoleucine and stimulated by valine. From this work, it is clear that the aspartate-derived amino-acid metabolism in Z. rouxii only partly resembles that in S. cerevisiae. Copyright (C) 2000 Elsevier Science Inc. To elucidate the growth inhibitory effect of threonine, the regulation of the aspartate-derived amino-acid metabolism in Zygosaccharomyces rouxii, an important yeast for the flavor development in soy sauce, was investigated. It was shown that threonine inhibited the growth of Z. rouxii by blocking the methionine synthesis. It seemed that threonine blocked this synthesis by inhibiting the conversion of aspartate. In addition, it was shown that the growth of Z. rouxii, unlike that of Saccharomyces cerevisiae, was not inhibited by the herbicide sulfometuron methyl (SMM). From enzyme assays, it was concluded that the acetohydroxy acid synthase in Z. rouxii, unlike that in S. cerevisiae, was not sensitive to SMM. Furthermore, the enzyme assays demonstrated that the activity of threonine deaminase in Z. rouxii, like in S. cerevisiae, was strongly inhibited by isoleucine and stimulated by valine. From this work, it is clear that the aspartate-derived amino-acid metabolism in Z. rouxii only partly resembles that in S. cerevisiae.
The fate of sulfonated aromatic amines under aerobic and anaerobic conditions and in an aerobic bioreactor system
Tan, N.C.G. ; Leeuwen, A. van; Voorthuizen, E.M. van; Lettinga, G. ; Field, J.A. - \ 2000
In: ISEB 4 Proceedings of the 4th International Symposium on Environmental Biotechnology, Noordwijkerhout, 10-12 April 2000 / S. Hartmans and P.N.L. Lens. - [S.l.] : [s.n.], 2000. - ISBN 90-6754-594-5 - p. 567 - 570.
A novel gene encoding xanthan lyase of Paenibacillus alginolyticus strain XL-1
Ruijssenaars, H.J. ; Hartmans, S. ; Verdoes, J.C. - \ 2000
Applied and Environmental Microbiology 66 (2000). - ISSN 0099-2240 - p. 3945 - 3950.
Xanthan-modifying enzymes are powerful tools in studying structure-function relationships of this polysaccharide. One of these modifying enzymes is xanthan lyase, which removes the terminal side chain residue of xanthan. In this paper, the cloning and sequencing of the first xanthan lyase-encoding gene is described, i.e., the xalA gene, encoding pyruvated mannose-specific xanthan lyase of Paenibacillus alginolyticus XL-1. The xalA gene encoded a 100,823-Da protein, including a 36-amino-acid signal sequence. The 96,887-Da mature enzyme could be expressed functionally in Escherichia coli. Like the native enzyme, the recombinant enzyme showed no activity on depyruvated xanthan. Compared to production by P. alginolyticus, a 30-fold increase in volumetric productivity of soluble xanthan lyase was achieved by heterologous production in E. coli. The recombinant xanthan lyase was used to produce modified xanthan, which showed a dramatic loss of the capacity to form gels with locust bean gum.
Biodegradability of food-associated extracellular polysaccharides
Ruijssenaars, H.J. ; Stingele, F. ; Hartmans, S. - \ 2000
Current Microbiology 40 (2000). - ISSN 0343-8651 - p. 194 - 199.
Fungal growth on toluene : Monitoring metabolic pathways with fluorinated analogues and 19F-NMR
Prenafeta-Boldu, F.X. ; Luykx, D.M.A.M. ; Vervoort, J. ; Bont, J.A.M. de - \ 2000
In: Proceedings of the 4th International Symposium on Environmental Biotechnology : 4th International Symposium on Environmental Biotechnology, Noordwijkerhout, NL, 2000 / S. Hartmans, P. Lens. - Wageningen : [s.n.], 2000. - ISBN 90-6754-594-5 - p. 418 03:B3 - 418 03:B3.
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