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Data included are related to the research article “Isolation of biofunctional bovine immunoglobulin G from milk- and colostral whey with mixed-mode chromatography at lab and pilot scale” (Heidebrecht et al., 2018) [1]. Data show individual bovine whey proteins in flow-through and elution fractions using different chromatographic resins as well as different binding and elution conditions. The relevant analytical methods for individual protein detection were SDS-PAGE and reversed phase- high performance liquid chromatography. The focus of the data is on the two mixed mode materials MEP HyperCel™ and Capto™-multimodal chromatography. Resins were used individually, in series and at different scale. Data provide information at which binding and elution conditions it is possible to isolate bovine IgG from milk and colostral whey and at which purity.

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Milk protein fractionation by microfiltration membranes is an established but still growing field in dairy technology. Even under cross-flow conditions, this filtration process is impaired by the formation of a deposit by the retained protein fraction, mainly casein micelles. Due to deposition formation and consequently increased overall filtration resistance, the mass flow of the smaller whey protein fraction declines within the first few minutes of filtration. Currently, there are only a handful of analytical techniques available for the direct observation of deposit formation with opaque feed media and membranes. Here, we report on the ongoing development of a non-invasive and non-destructive method based on magnetic resonance imaging (MRI), and its application to characterise deposit layer formation during milk protein fractionation in ceramic hollow fibre membranes as a function of filtration pressure and temperature, temporally and spatially resolved. In addition, the chemical composition of the deposit was analysed by reversed phase high pressure liquid chromatography (RP-HPLC). We correlate the structural information gained by in-situ MRI with the protein amount and composition of the deposit layer obtained by RP-HPLC. We show that the combination of in-situ MRI and chemical analysis by RP-HPLC has the potential to allow for a better scientific understanding of the pressure and temperature dependence of deposit layer formation.

The fractionation efficiency of hollow fiber membranes (HFM) for milk protein fractionation was compared to ceramic tubular membranes (CTM) and spiral wound membranes (SWM). HFM combine the features of high membrane packing density of SWM and the more defined flow conditions and better control of membrane fouling in the open flow channel cross-sections of CTM. The aim was to comparatively analyze the effect of variations in local pressure and flow conditions while using single industrially sized standard modules with similar dimensions and module footprints (module diameter and length). The comparative assessment with varied transmembrane pressure was first applied for a constant feed volume flow rate of 20 m3 h−1 and, secondly, with the same axial pressure drop along the modules of 1.3 bar m−1, similar to commonly applied crossflow velocity and wall shear stress conditions at the industrial level. Flux, transmission factor of proteins (whey proteins and serum caseins), and specific protein mass flow per area membrane and per volume of module installed were determined as the evaluation criteria. The casein-to-whey protein ratios were calculated as a measure for protein fractionation effect. Results obtained show that HFM, which so far are under-represented as standard module types in industrial dairy applications, appear to be a competitive alternative to SWM and CTM for milk protein fractionation.