Výsledky vyhledávání - "Jongh, H.H.J. de"

Effect of heat treatment on the conformational stability of intact and cleaved forms of the peanut allergen Ara h 6 in relation to its IgE-binding potency

Autor: Jongh, H.H.J. de, Jong, G.A.H. de, Apostolovic, D., Taylor, S.L., Baumert, J.L., Koppelman, S.J.

Publikováno v: Food Chemistry, 326

This work reports on the effect of heat treatment on the protein conformational stability of intact and post-translationally cleaved peanut allergen Ara h 6 in relation to IgE-binding. Intact and post-translationally cleaved Ara h 6 are structurally

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Fibril Formation from Pea Protein and Subsequent Gel Formation

Autor: Munialo, XC.D., Martin, A.H., Linden, E. van der, Jongh, H.H.J de

Publikováno v: Journal of Agricultural and Food Chemistry, 62, 2418−2427

The objective of this study was to characterize fibrillar aggregates made using pea proteins, to assemble formed fibrils into protein-based gels, and to study the rheological behavior of these gels. Micrometer-long fibrillar aggregates were observed

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Structure of mixed β-lactoglobulin/pectin adsorbed layers at air/water interfaces; a spectroscopy study

Autor: Ganzevles, R.A., Fokkink, R., Vliet, T. van, Cohen Stuart, M.A., Jongh, H.H.J. de

Publikováno v: Journal of Colloid and Interface Science, 1, 317, 137-147

Based on earlier reported surface rheological behaviour two factors appeared to be important for the functional behaviour of mixed protein/polysaccharide adsorbed layers at air/water interfaces: (1) protein/polysaccharide mixing ratio and (2) formati

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Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

Autor: Teeffelen, A.M.M. van, Broersen, K., Jongh, H.H.J. de

Publikováno v: Protein Science, 8, 14, 2187-2194

Chemical glycosylation of proteins occurs in vivo spontaneously, especially under stress conditions, and has been linked in a number of cases to diseases related to protein denaturation and aggregation. It is the aim of this work to study the origin

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Identification of pitfalls in the analysis of heat capacity changes of β-lactoglobulin A

Autor: Teeffelen, A.M.M. van, Meinders, M.B.J., Jongh, H.H.J. de

Publikováno v: International Journal of Biological Macromolecules, 1-2, 37, 28-34

Information on changes in heat capacity (ΔCp) of proteins upon unfolding is used frequently in literature to understand possible follow-up reactions of protein denaturation, like their aggregation propensity. This thermodynamic property is intrinsic

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Protein Exposed Hydrophobicity Reduces the Kinetic Barrier for Adsorption of Ovalbumin to the Air-Water Interface

Autor: Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, F.A.G.J., Jongh, H.H.J. de

Publikováno v: Langmuir, 21, 19, 8964-8970

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 foll

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