Searched for: author%3A%22de+Jongh%2C+H.H.J.%22
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Kudryashova, E.V. (author), Meinders, M.B.J. (author), Visser, A.J.W.G. (author), van Hoek, A. (author), de Jongh, H.H.J. (author)
The molecular properties of egg white ovalbumin adsorbed at the air/water interface were studied using infrared reflection absorption spectroscopy (IRRAS) and time-resolved fluorescence anisotropy (TRFA) techniques. Ovalbumin adsorbed at the air/ water interface adopts a characteristic partially unfolded conformation in which the content of the...
article 2003
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Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Paques, M. (author), van Vliet, T. (author), Gruppen, H. (author), Voragen, A.G.J. (author), Centre for Protein Technology TNO-WU (author)
Formation and structure of glycinin gels were studied in relation to protein conformation for two pH values and three ionic strengths. While at I = 0.03 the gels were found to be fine stranded, gel coarseness increased when the ionic strength was higher. At I = 0.03 finer gel network structures were formed at pH 3.8 than at pH 7.6, whereas for I...
article 2003
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de Groot, J. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
The aim of this work was to study the effect of the formation of more heat-stable conformers of chicken egg ovalbumin during incubation at basic pH (9.9) and elevated temperature (55°C) on the protein aggregation properties at neutral pH. Native ovalbumin (N-OVA) is converted on the hours time-scale into more heat-stable forms denoted I- ...
article 2003
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Wierenga, P.A. (author), Meinders, M.B.J. (author), Egmond, M.R. (author), Voragen, F.A.G.J. (author), de Jongh, H.H.J. (author)
Using native and caprylated ovalbumin, the role of exposed hydrophobicity on the kinetics of protein adsorption to the air - water interface is studied. First, changes in the chemical properties of the protein upon caprylation were characterized followed by measurement of the changes in adsorption kinetics. No change in the molecular structure...
article 2003
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Koppelman, S.J. (author), van Koningsveld, G.A. (author), Knulst, A.C. (author), Gruppen, H. (author), Pigmans, I.G.A.J. (author), de Jongh, H.H.J. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
The interaction of the major potato allergen patatin, Sol t 1, with IgE was investigated on a quantitative level as a function of heat treatment at different temperatures. On the basis of a number of publications, potato is considered to be a heat-labile allergen, but the molecular explanation for this behavior was not given. In this work, heat...
article 2002
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Simons, J.-W. (author), Simons, F.A. (author), Kosters, H.A. (author), Visschers, R.W. (author), de Jongh, H.H.J. (author), TNO Voeding (author)
article 2002
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van Koningsveld, G.A. (author), Gruppen, H. (author), de Jongh, H.H.J. (author), Wijngaards, G. (author), van Boekel, M.A.J.S. (author), Walstra, P. (author), Voragen, A.G.J. (author), TNO Voeding (author)
article 2002
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van Koningsveld, G.A. (author), Gruppen, H. (author), de Jongh, H.H.J. (author), Wijngaards, G. (author), van Boekel, M.A.J.S. (author), Walstra, P. (author), Voragen, A.G.J. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
The effects of pH and various additives on the precipitation and (re)solubility at pH 7 of potato proteins from industrial potato fruit juice (PFJ) were studied. The use of various strong and weak acids did not result in differences in protein precipitation, which on average occurred to a maximum of 60% of total protein at pH 3. Weak acids did,...
article 2002
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Alting, A.C. (author), de Jongh, H.H.J. (author), Visschers, R.W. (author), Simons, J.W.F.A. (author), TNO Voeding (author)
article 2002
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TNO Voeding (author), Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Gruppen, H. (author), Voragen, A.G.J. (author)
In heat denaturation studies conducted in the past the genetic variants of glycinin have been considered as a homogeneous group of proteins. In this work the validity of this assumption was tested. It was found by calorimetric studies that glycinin denatures heterogeneously at pH 7.6. When the temperature of isothermal treatment is increased...
article 2002
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de Jongh, H.H.J. (author), Meinders, M.B.J. (author), TNO Voeding (author)
article 2002
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van Koningsveld, G.A. (author), Gruppen, H. (author), de Jongh, H.H.J. (author), Wijngaards, G. (author), van Boekel, M.A.J.S. (author), Walstra, P. (author), Voragen, A.G.J. (author), TNO Voeding (author)
article 2001
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TNO Voeding (author), Renkema, J.M.S. (author), Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Gruppen, H. (author), van Vliet, T. (author)
This study is focussed on the influence of pH on the gel forming properties of soy protein isolate and purified glycinin in relation to denaturation and aggregation. At pH 7.6 more fine-stranded gels were formed characterised by low G' values, and a smooth, slightly turbid appearance, whereas at pH 3.8 coarse gels were obtained with a high...
article 2000
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Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Hessing, M. (author), Gruppen, H. (author), Voragen, A.G.J. (author)
The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxxxxxx) at ambient temperatures influences heat denaturation. It is found that the 7S form of glycinin denatures at a lower temperature than the 11S form, as demonstrated by a combination of calorimetric (DSC) and circular dichroism (CD) experiments. At...
article 2000
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TNO Voeding (author), Lakemond, C.M.M. (author), de Jongh, H.H.J. (author), Hessing, M. (author), Gruppen, H. (author), Voragen, A.G.J. (author)
This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a quaternary, tertiary, and secondary folding level under conditions representative for food products. When the ionic strength is lowered from 0.5 to 0.2 or 0.03, the basic polypeptides shift more to the exterior of the...
article 2000
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Caessens, P.W.J.R. (author), de Jongh, H.H.J. (author), Norde, W. (author), Gruppen, H. (author), TNO Voeding (author)
Changes in the secondary structure upon adsorption of β-casein (βCN) and of distinct parts of its sequence were investigated by far-ultraviolet circular dichroism in order to find suggested relationships with foam and emulsion-forming and -stabilising properties of the same protein/peptides. A teflon/water interface was used as a model system...
article 1999
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Koppelman, S.J. (author), Bruijnzeel-Koomen, C.A.F.M. (author), Hessing, M. (author), de Jongh, H.H.J. (author)
Ara h 1, a major peanut allergen was isolated, and its structure on secondary, tertiary, and quaternary level at ambient temperature was investigated using spectroscopic and biochemical techniques. Ara h 1 appeared to be a highly structured protein on a secondary level, possesses a clear tertiary fold, and is present as a trimeric complex. Heat...
article 1999
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TNO Voeding (author), Pots, A.M. (author), Gruppen, H. (author), de Jongh, H.H.J. (author), van Boekel, M.A.J.S. (author), Walstra, P. (author), Voragen, A.G.J. (author)
A kinetic model of the thermal aggregation of patatin is presented based on chromatographic analysis of the proportions of nonaggregated and aggregated patatin. It was observed that the decrease of the amount of nonaggregated patatin proceeded initially quickly and was followed by slower aggregation at longer incubation times. It was shown that...
article 1999
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Pots, A.M. (author), de Jongh, H.H.J. (author), Gruppen, H. (author), Hessing, M. (author), Voragen, A.G.J. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
This paper presents the structural stability of patatin, the major potato (Solanum tuberosum cv. Bintje) tuber protein. Using far- and near-ultraviolet circular dichroism and fluorescence spectroscopy, the conformation of patatin was studied under various conditions as a function of temperature. Patatin is a protein that unfolds partly due to...
article 1998
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Pots, A.M. (author), de Jongh, H.H.J. (author), Gruppen, H. (author), Hamer, R.J. (author), Voragen, A.G.J. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
This paper presents a first structural characterization of isolated patatin, the major potato tuber protein, at ambient and elevated temperatures. Isolated patatin at room temperature is a highly structured molecule at both secondary and tertiary levels. It is estimated from far-ultraviolet circular dichroism data that about 33% of the residues...
article 1998
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