Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Roy J.B.M. Delahaije"'
Autor:
Christiane Rösch, Marjolein Meijerink, Roy J.B.M. Delahaije, Nico Taverne, Harry Gruppen, Jerry M. Wells, Henk A. Schols
Publikováno v:
Journal of Functional Foods, Vol 26, Iss , Pp 279-289 (2016)
Specific structures of oat and barley β(1,3)(1,4)-glucans induced different in vitro immunomodulatory effects in bone marrow derived dendritic cells (BMDC) from TLR2/4 knock out mice. All barley β-glucan fractions induced larger amounts of cytokine
Externí odkaz:
https://doaj.org/article/16b14cb3837b4403904933b4fbdcf59b
Publikováno v:
Food Hydrocolloids, 125
Food Hydrocolloids 125 (2022)
Food Hydrocolloids 125 (2022)
In this study, we explored how substituting whey protein isolate (WPI) with soy protein isolate (SPI) affects the linear and non-linear rheological behavior of acid-induced gels, and their microstructures. Commercial SPI and WPI dispersions (pH 7.0,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9710ddc8c642e96760cff7abd4249c57
https://research.wur.nl/en/publications/acid-induced-gels-from-soy-and-whey-protein-thermally-induced-mix
https://research.wur.nl/en/publications/acid-induced-gels-from-soy-and-whey-protein-thermally-induced-mix
Publikováno v:
Food Hydrocolloids 91 (2019)
Food Hydrocolloids, 91, 263-274
Food Hydrocolloids, 91, 263-274
The effect of temperature (below denaturation temperature) on protein foam formation and stabilization is potentially large, but has received little attention. This study aims to identify the effect of temperature (15–60 °C) on ovalbumin-stabilize
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd1e08b83a86bcfabda73a0e7a9fc457
https://doi.org/10.1016/j.foodhyd.2019.01.030
https://doi.org/10.1016/j.foodhyd.2019.01.030
Autor:
Roy J.B.M. Delahaije, Leonardo Cornacchia, Harry Gruppen, Evelien L. van Boxtel, Peter A. Wierenga
Publikováno v:
Journal of Agricultural and Food Chemistry, 64(21), 4362-4370
Journal of Agricultural and Food Chemistry 64 (2016) 21
Journal of Agricultural and Food Chemistry 64 (2016) 21
The amount of heat-denatured whey protein is typically determined by pH 4.6 precipitation. Using this method, a significant amount of nondenatured protein was reported even after long heating times. Apparently, a fraction of the unfolded protein refo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8e03e70430ae67eab4789f341adef9
https://doi.org/10.1021/acs.jafc.6b00816
https://doi.org/10.1021/acs.jafc.6b00816
Publikováno v:
Journal of Agricultural and Food Chemistry 63 (2015) 21
Journal of Agricultural and Food Chemistry, 63(21), 5257-5265
Journal of Agricultural and Food Chemistry, 63(21), 5257-5265
Typically, heat-induced aggregation of proteins is studied using a single protein under various conditions (e.g., temperature). Because different studies use different conditions and methods, a mechanistic relationship between molecular properties an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::489aa3ae942d7a7dba0d64fa9b817199
https://doi.org/10.1021/acs.jafc.5b00927
https://doi.org/10.1021/acs.jafc.5b00927
Publikováno v:
Journal of Colloid and Interface Science, 430, 69-77
Journal of Colloid and Interface Science 430 (2014)
Journal of Colloid and Interface Science 430 (2014)
This study investigates the influence of succinylation on the molecular properties (i.e. charge, structure and hydrophobicity) and the flocculation behavior of patatin-stabilized oil-in-water emulsions. Patatin was succinylated to five degrees (0% (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c45b3644aebc7d819b616323dcbaf455
https://doi.org/10.1016/j.jcis.2014.05.019
https://doi.org/10.1016/j.jcis.2014.05.019
Autor:
Roy J.B.M. Delahaije, Jerry M. Wells, Harry Gruppen, Christiane Rösch, Henk A. Schols, Nico Taverne, Marjolein Meijerink
Publikováno v:
Journal of Functional Foods 26 (2016)
Journal of Functional Foods, 26, 279-289
Journal of Functional Foods, Vol 26, Iss, Pp 279-289 (2016)
Journal of Functional Foods, 26, 279-289
Journal of Functional Foods, Vol 26, Iss, Pp 279-289 (2016)
Specific structures of oat and barley β(1,3)(1,4)-glucans induced different in vitro immunomodulatory effects in bone marrow derived dendritic cells (BMDC) from TLR2/4 knock out mice. All barley β-glucan fractions induced larger amounts of cytokine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a98a870b2ff0d8be981ee299c0906cb
Autor:
Roy J.B.M. Delahaije, Harry Gruppen, Frederik J. Lech, Marcel B.J. Meinders, Peter A. Wierenga
Publikováno v:
Food Hydrocolloids, 57, 46-54
Food Hydrocolloids 57 (2016)
Food Hydrocolloids 57 (2016)
To understand the properties of protein stabilized foam, quantitative parameters, such as the concentration dependence of the foam properties need to be determined. Recently, a concept was proposed that predicts the emulsifying ability (i.e. the drop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a658d51654617943916d343cc078b466
https://research.wur.nl/en/publications/identification-of-critical-concentrations-determining-foam-abilit
https://research.wur.nl/en/publications/identification-of-critical-concentrations-determining-foam-abilit
Autor:
Roy J.B.M. Delahaije, Harry Gruppen, Surender Kumar Dhayal, Peter A. Wierenga, Renko de Vries
Publikováno v:
Soft Matter 11 (2015) 40
Soft Matter, 11(40), 7888-7898
Soft Matter, 11(40), 7888-7898
Hard colloidal nanoparticles (e.g. partly hydrophobised silica), are known to make foams with very high foam-stability. Nanoparticles can also be produced from proteins by enzymatic cross-linking. Such protein based particles are more suitable for fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a3c6369d8b1217a57885537663059c2
https://research.wur.nl/en/publications/enzymatic-cross-linking-of-a-lactalbumin-to-produce-nanoparticles
https://research.wur.nl/en/publications/enzymatic-cross-linking-of-a-lactalbumin-to-produce-nanoparticles
Publikováno v:
Colloids and Surfaces. B: Biointerfaces, 123, 199-206
Colloids and Surfaces. B: Biointerfaces 123 (2014)
Colloids and Surfaces. B: Biointerfaces 123 (2014)
The adsorption behaviour of proteins depends significantly on their molecular properties and system conditions. To study this relation, the effect of relative exposed hydrophobicity, protein concentration and ionic strength on the adsorption rate and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7dc60f53145b10477b9a903789233f9
https://pubmed.ncbi.nlm.nih.gov/25280607
https://pubmed.ncbi.nlm.nih.gov/25280607