Potential and Challenges of a Targeted Membrane Pre-Fouling: Process Performance of Milk Protein Fractionation After the Application of a Transglutaminase Treatment of Casein Micelles
2025
Michael Reitmaier | Ulrich Kulozik | Petra Först
The covalent cross-linking of caseins by the enzyme transglutaminase (Tgase) stabilizes the structure of casein micelles. In our study, the effects of a pretreatment of skim milk (SM) by Tgase on milk protein fractionation by microfiltration were tested. Tgase was found to induce amount-dependent modifications of all milk proteins in SM and a reduction in deposit resistance for laboratory dead-end filtrations of up to 20%. This improvement in process performance could partially be confirmed in pilot-scale cross-flow filtrations of Tgase-pretreated SM and micellar casein solutions (MCC). These comparative trials with untreated retentates under a variation of &Delta:pTM (0.5&ndash:2 bar) at 10 and 50°: revealed distinct differences in deposit behavior and achieved the reduction in deposit resistance in a range of 0&ndash:20%. The possibility of pre-fouling with enzymatically pretreated MCC prior to SM filtration was also investigated. Under different pre-fouling conditions, practical modes of retentate change, and pre-foulant compositions, a switch to untreated SM consistently resulted in an immediate and major increase in deposit resistance by 50&ndash:150%. This was partially related to the change in the ionic environment and the protein fraction. Nevertheless, our results underline the potential of Tgase pretreatment and pre-fouling approaches to alter filtration performance for different applications.
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