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P. Van der Meeren

Researcher at Ghent University

Publications -  55
Citations -  1917

P. Van der Meeren is an academic researcher from Ghent University. The author has contributed to research in topics: Whey protein & Membrane. The author has an hindex of 23, co-authored 55 publications receiving 1720 citations. Previous affiliations of P. Van der Meeren include National Fund for Scientific Research.

Papers
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Characterization of polymeric nanofiltration membranes for systematic analysis of membrane performance

TL;DR: In this article, a comparison of three different nanofiltration membranes, namely, NF-270, NB-90 and NB-30XLE, was performed, and the results showed that the NB 30XLE showed the highest surface charge density and the smallest pore blocking.
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Characterization of commercial nanofiltration membranes and comparison with self-made polyethersulfone membranes

TL;DR: In this paper, six different polymeric nanofiltration (NF) membranes (UTC20, N30F, NTR7450 and NFPES10) were characterized using atomic force microscopy (AFM) in noncontact and tapping modes.
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Influence of membrane and colloid characteristics on fouling of nanofiltration membranes

TL;DR: In this article, the effects of fouling for several representative nanofiltration membranes during filtration of several types of colloids in different circumstances (pH, ionic strength) are presented.
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Accurate particle size distribution determination by nanoparticle tracking analysis based on 2-D Brownian dynamics simulation.

TL;DR: Simulation of a step length distribution allows obtaining a much more reliable estimation of the particle size distribution, thereby reducing the artificial broadening of the distribution, as is typically observed by direct conversion of step length to particle size data.
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Improved emulsion stabilizing properties of whey protein isolate by conjugation with pectins

TL;DR: The results indicated that the dry heat-induced covalent binding of low methoxyl pectin to whey protein, as shown by SDS-PAGE, led to a substantial improvement in the emulsifying behaviour at pH 5.5, which is near the isoelectric pH of the main protein β-lactoglobulin.