Spacer design in spiral-wound membranes (SWMs) significantly affects the axial pressure drop in the flow channel but also the deposit layer removal. However, the effects of the spacer design and feed flow distribution in the module on the filtration performance have not yet been investigated during the highly fouling-susceptible fractionation of proteins from skim milk by SWMs. Therefore, a parallel spacer with no turbulence promotion and a less homogeneous feed flow distribution in the SWM was compared to a diamond spacer with regard to its impact on deposit formation and filtration performance. The experiments were conducted in a flat sheet test cell and in SWMs. The parallel spacer induced a more homogeneous deposit layer formation. However, no difference in filtration performance could be observed in the experiments with the test cell. Even though deposit layer formation dominates the microfiltration, its amount and spatial distribution could not be directly linked to the filtration performance. Furthermore, both spacers were assessed in SWM. Despite the higher crossflow velocity applicable in the more open channels of the parallel spacer, the performance of the parallel spacer was inferior to the diamond spacer. This was independent of the viscosity of the feed. Due to the high curvature of the membrane sheets close to the permeate collection tube, the cross-section of the flow channels in the SWM equipped with the parallel spacer was reduced. This resulted in a distinctly lower deposit layer control and performance, which could not be compensated by the resulting higher crossflow velocity far from the permeate collection tube.

Disulfide formation of whey proteins during heat treatment via thiol oxidation is important with regard to techno-functional properties. Due to the formation of other oxidation products than disulfides, the decrease in free thiol concentration is not proportional to the disulfide formation. Thus, in order to evaluate thiol reactivity and disulfide concentration both parameters are required. Currently applied methods focus mainly on the loss of free thiols using the spectrophotometric Ellman's assay. Next to that, we improved an existing RP-HPLC assay using the thiol reagent 4,4′-Dithiodipyridine (DTDP) to quantify free thiols as well as total (free thiols and disulfide bonds) thiols of native and heat-treated whey proteins. Thereby, the sample preparation technique, the sample handling, and the analysis technique were optimized. Thus, the paper provides a simple RP-HPLC method for quantification of thiol oxidation reactions to determine heat-induced changes in the structure of whey proteins. In addition, the method should be applicable to other protein systems due to the method validation by proteins of different amounts of free and total thiols in their structure.•Simple RP-HPLC method for quantification of free and total thiols using 4,4′-Dithiodipyridine (DTDP).•High recovery rates for free and total thiols.•High stability within 24 h.

It is widely accepted that protein-based particles can efficiently stabilize foams and emulsions. However, it is not fully elucidated which particle properties are decisive for the stabilization of air/water and oil/water interfaces. To unravel this correlation, selected properties of nano-sized soluble β-lactoglobulin particles were changed one at a time. Therefore, particles of (1) variable size but similar zeta potential and degree of cross-linking and (2) similar size but different further properties were produced by heat treatment under a specific combination of pH value and NaCl concentration and then analyzed for their interfacial behavior as well as foaming and emulsifying properties. On the one hand, it was found that the initial phase of protein adsorption at both the air/water and the oil/water interface was mainly influenced by the zeta potential, independent of the particle size. On the other hand, foam stability as resolved from the time-dependent evolution of mean bubble area negatively correlated with disulfide cross-linking, whereas emulsion stability in terms of oil droplet flocculation showed a positive correlation with disulfide cross-linking. In addition, flocculation was more pronounced for larger particles. Concluding from this, foam and emulsion stability are not linked to the same particle properties and, thus, explanatory approaches cannot be used interchangeably.

Fouling distinctly reduces the filtration performance of membranes. A characterization of the fouling in membranes, however, is difficult due to its spatial distribution. Currently applied methods for deposit layer analysis are rather complex or do not offer a spatial resolution. Knowledge of the spatial distribution, however, could be used to improve the design of membranes, modules, and spacers. Staining with Coomassie Brilliant Blue, related to the staining of PAGE gels, is a simple method to visualize and analyze the deposited proteins semi-quantitatively. We improved an existing staining technique for protein deposits on membranes by adding a calibration for the semi-quantitative analysis and optimizing the sample handling. The method provides a spatially resolved analysis of deposited proteins up to a concentration of 10 g m^-2. Apart from staining, data processing is described in order to generate false colors or topographic images of deposits. Thus, the paper describes a simple method to assess and visualize the influence of module characteristics such as spacer design on the spatially resolved protein fouling of polymeric and ceramic membranes. Therefore, the method can contribute to the improvement of the module design and processing conditions with regard to the filtration performance. •Visualization of proteinaceous deposits on membranes•Spatially resolved quantification of proteinaceous deposits.