Remco Kornet

ORCID: 0000-0001-7493-4090
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About
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Research Areas
  • Proteins in Food Systems
  • Microencapsulation and Drying Processes
  • Polysaccharides Composition and Applications
  • Pickering emulsions and particle stabilization
  • Food composition and properties
  • Phytase and its Applications
  • Legume Nitrogen Fixing Symbiosis
  • Enzyme Production and Characterization
  • African Botany and Ecology Studies
  • Microbial Metabolites in Food Biotechnology
  • Protein Hydrolysis and Bioactive Peptides
  • Plant Reproductive Biology
  • Muscle metabolism and nutrition

Wageningen University & Research
2019-2024

TiFN
2019-2024

The transition from animal- to plant-derived dietary proteins is of global importance. Plant are normally processed into extracts, and due the type process, globulin class mainly extracted. Such extractions have several waste streams, containing another protein class: albumins. Here, we show that plant albumins good functionality. We compared interfacial foaming properties globulins mung bean, Bambara groundnut yellow pea. were good, similar or even superior those whey egg white proteins,...

10.1016/j.foostr.2022.100254 article EN cc-by Food Structure 2022-01-01

Some studies have shown that mild fractionation may result in similar or even better functional properties, than those of highly purified ingredients. This study aimed to relate the level aqueous purification composition, solubility and viscosity yellow pea fractions. A seldomly used method cryo-planing combined with Cryo-SEM revealed presence protein bodies starch granules seeds flour, sizes ~3 μm ~20 μm, respectively. Fractions purities ranging from 40 85% (w/w) were obtained flour...

10.1016/j.foodhyd.2019.105332 article EN cc-by-nc-nd Food Hydrocolloids 2019-08-23

Limited fractionation of yellow pea yielded functional protein fractions with higher gelling capacity. Pea concentrates were obtained by dispersing flour at unadjusted pH (~6.7) and 8. An additional isoelectric precipitation step resulted in a protein-rich isolate protein-poor supernatant. Aqueous solutions these (up to 15 wt %) heated from 20 95 subsequently cooled °C, their viscoelastic response was characterized small large amplitude oscillatory shear measurements (SAOS LAOS,...

10.1016/j.foodhyd.2020.106285 article EN cc-by-nc-nd Food Hydrocolloids 2020-08-28

Specific pea protein fractionation steps can be used to control foaming and emulsifying properties of three fractions at pH 7.0. Mild fractionation, involving dispersion the flour 8.0, subsequent centrifugation, drying supernatant yielded a concentrate (PPC). Further was achieved by applying isoelectric precipitation on supernatant, followed re-dispersion, resulting in globulin-rich fraction (GLB-RF); – which could considered by-product diafiltrated obtain albumin-rich (ALB-RF). Size...

10.1016/j.foodhyd.2021.107456 article EN cc-by Food Hydrocolloids 2021-12-16

In this study we investigated the effect of different aqueous fractionation processes on suitability pea protein isolates (PPI) to substitute whey isolate (WPI) in heat-set gels. We found that a milder process based diafiltration was successful substituting WPI, yielding similar gel strength (i.e. elastic modulus) at range concentrations. Three were analysed, one obtained using (PPId), another isoelectric precipitation (PPIp), and commercial (PPIc) as reference. The PPIp PPId contained...

10.1016/j.foodhyd.2021.106691 article EN cc-by-nc-nd Food Hydrocolloids 2021-02-21

Currently, plant proteins are fractionated to ingredients with high purities, but an often ignored point is the impact of extraction and fractionation process on protein functionality. To allow a fair effective comparison, it key understand changes in protein's aggregated state occurring extracted during processing. We review conventional upcoming processes (on pulses oilseeds) focus how processing history influences macroscopic functional properties proteins. establish this link, we dive...

10.1016/j.foodhyd.2024.110223 article EN cc-by Food Hydrocolloids 2024-05-22

In this study we explored the gelling behaviour of a pea protein concentrate (PPC), an albumin-fraction (ALB-F) and globulin-rich fraction (GLB-RF), in comparison with as substitute for whey isolate (WPI), by small oscillatory large amplitude shear (SAOS LAOS) rheology. It was found that PPC formed firmest gels (defined highest elastic modulus), but gel not firm pure WPI gel. The ALB-F weakest due to its low purity. For better view on albumin behaviour, further diafiltrated albumin-enriched...

10.1016/j.foodhyd.2021.106891 article EN cc-by-nc-nd Food Hydrocolloids 2021-05-12

Legumes such as pea and soy have the ability to form coacervates in solution, which depends on pH salt concentration. We studied phenomenon of coacervation for protein solutions proteins were exposed different extents fractionation (i.e., neutral extraction, extraction followed by freeze drying, alkaline isoelectric precipitation). The dispersed fractions was varied between 5.5 6.5 concentration 0 500 mM NaCl. Confocal microscopy particle size measurements used confirm presence spherical...

10.1016/j.foodhyd.2021.107379 article EN cc-by-nc-nd Food Hydrocolloids 2021-11-19

Plant proteins, after extraction from sources such as pea can be used functional ingredients in emulsions and gels. However, the protein fractionation route affects functionality. We investigated differences rheological properties of emulsion-filled gel (EFGs) structured by isolate obtained using either isoelectric precipitation (PPIp) or diafiltration (PPId), at varying pH oil content. PPIp PPId had a content 75.3 77.7 wt %, respectively. first studied oil-water interfacial rheology...

10.1016/j.foodhyd.2021.107427 article EN cc-by Food Hydrocolloids 2021-12-06

We investigated the complementary roles of napins and cruciferins present in a rapeseed protein mixture (RPM) structuring emulsion-filled gels (EFGs). Napins are small molecular weight albumins with high interfacial activity, while globulins that form upon heat-induced gelation. The role is to stabilize emulsion droplets, cruciferins, which were previously found interact adsorbed napin layer, can build gel network around droplets. effects oil concentration (0–30 wt%) pH (5 7) on rheological...

10.1016/j.foodhyd.2021.107400 article EN cc-by Food Hydrocolloids 2021-11-24
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