Searched for: author%3A%22van+den+Broek%2C+L.A.M.%22
(1 - 11 of 11)
document
van Boxtel, E.L. (author), Koppelman, S.J. (author), van den Broek, L.A.M. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80-110 °C, depending on the pH. Upon heating above its denaturation...
article 2008
document
van Boxtel, E.L. (author), van den Broek, L.A.M. (author), Koppelman, S.J. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Legumin proteins Ara h 3 from peanuts and glycinin from soybeans are increasingly described as important allergens. The stability of an allergen's IgE binding capacity towards heating and digestion is considered an important characteristic for food allergens. We investigated the effects of heating and digestion on the IgE binding of Ara h 3 and...
article 2008
document
van Boxtel, E.L. (author), Koppelman, S.J. (author), van den Broek, L.A.M. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author), KvL (author)
This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, oligomeric Ara h 1, either unheated or preheated,...
article 2008
document
van Boxtel, E.L. (author), van den Broek, L.A.M. (author), Koppelman, S.J. (author), Vincken, J.-P. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Mildly extracted peanut allergen Ara h 1 was previously reported to occur as an oligomeric complex. In this paper we describe how the protein in this oligomeric complex interacts noncovalently with phenolic compounds of the proanthocyanidin type. These interactions are being disrupted during anion exchange chromatography, resulting in the...
article 2007
document
van Boxtel, E.L. (author), van Beers, M.M.C. (author), Koppelman, S.J. (author), van den Broek, L.A.M. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration...
article 2006
document
van Boxtel, E.L. (author), van Koningsveld, G.A. (author), Koppelman, S.J. (author), van den Broek, L.A.M. (author), Voragen, A.G.J. (author), Gruppen, H. (author), TNO Kwaliteit van Leven (author)
A new, fast, large-scale purification method for Ber e 1, the major allergen from Brazil nuts, using expanded bed adsorption (EBA) chromatography, is presented. Using EBA, crude extracts can be applied to a fluidized column, which allows the unhindered passage of particulate impurities, thereby avoiding time-consuming centrifugation or...
article 2006
document
Pouvreau, L. (author), Gruppen, H. (author), van Koningsveld, G. (author), van den Broek, L.A.M. (author), Voragen, A.G.J. (author), TNO Voeding (author)
The thermal unfolding of potato serine protease inhibitor (PSPI), the most abundant protease inhibitor group in potato tuber, was measured using far UV CD spectroscopy, fluorescence spectroscopy, and DSC. The results indicate that the thermal as well as the guanidinium-induced unfolding of PSPI occurs via a non-two-state mechanism in which at...
article 2005
document
Centraal Instituut voor Voedingsonderzoek TNO (author), Pouvreau, L. (author), Gruppen, H. (author), van Koningsveld, G.A. (author), van den Broek, L.A.M. (author), Voragen, A.G.J. (author)
Potato serine protease inhibitor (PSPI) is the most abundant protease inhibitor group in potato tuber. The investigated PSPI isoforms have a highly similar structure at both the secondary and the tertiary level. From the results described, PSPI is classified as a β-II protein based on (1) the presence in the near-UV spectra of sharp peaks,...
article 2004
document
TNO Zeist (author), van den Broek, L.A.M. (author), Pouvreau, L. (author), Lommerse, G. (author), Schipper, B. (author), van Koningsveld, G.A. (author), Gruppen, H. (author)
In the present study the structural properties of potato protease inhibitor 1 (PI-1) were studied as a function of temperature to elucidate its precipitation mechanism upon heating. A cDNA coding for PI-1 from cv. Bintje was cloned and expressed in Pichia pastoris. Using the recombinant PI-1 it was suggested that PI-1 behaves as a hexameric...
article 2004
document
TNO Voeding (author), Pouvreau, L. (author), Gruppen, H. (author), van Koningsveld, G.A. (author), van den Broek, L.A.M. (author), Voragen, A.G.J. (author)
The gene of the most abundant protease inhibitor in potato cv. Elkana was isolated and sequenced. The deduced amino acid sequence of this gene showed 98% identity with potato serine protease inhibitor (PSPI), a member of the Kunitz family. Therefore, the most abundant protease inhibitor was considered to be one of the isoforms of PSPI. The PSPI...
article 2003
document
Pouvreau, L. (author), Gruppen, H. (author), Piersma, S.R. (author), van den Broek, L.A.M. (author), van Koningsveld, G.A. (author), Voragen, A.G.J. (author), TNO Voeding (author)
article 2001
Searched for: author%3A%22van+den+Broek%2C+L.A.M.%22
(1 - 11 of 11)