Abstract

Proteins are one of the primary building blocks that have significant functional properties to be applied in food and pharmaceutical industries. Proteins could be beneficial in their concentrated products or isolates, of which membrane-based filtration methods such as ultrafiltration (UF) encompass application in broad spectra of protein sources. More importantly, selective enrichment by UF is of immense interest due to the presence of antinutrients that may dominate their perspicuous bioactivities. UF process is primarily obstructed by concentration polarization and fouling; in turn, a trade-off between productivity and selectivity emerges, especially when pure isolates are an ultimate goal. Several factors such as operating conditions and membrane equipment could leverage those pervasive contributions; therefore, UF protocols should be optimized for each unique protein mixture and mode of configuration. For instance, employing charged UF membranes or combining UF membranes with electrodialysis enables efficient separation of proteins with a similar molecular weight, which is hard to achieve by the conventional UF membrane. Meanwhile, some proposed strategies, such as utilizing ultrasonic waves, tuning operating conditions, and modifying membrane surfaces, can effectively mitigate fouling issues. A plethora of advancements in UF, from their membrane material modification to the arrangement of new configurations, contribute to the quest to actualize promising potentials of protein separation by UF, and they are reviewed in this paper.

Highlights

  • Proteins are essential to maintain proper energy density of living beings, along with regulating activities of enzymes pertinent to type-2 diabetes, hypertension, and stress relief [1]

  • Fractionation and/or purification of proteins in the range of 0.1–5 μm could be fractionated by charged UF, peptides around 1–10 μm by membrane chromatography, and that with 0.1–5 nm in size may be gathered by ultrasound (US)-assisted UF, high-performance tangential flow filtration (HPTFF), electro-UF membrane (EUF), electrodialysis with UF membrane (EDUF), and electrodialysis with bipolar membrane (EDBM) [18,19]

  • We focus on novel technologies of UF, with special attention in protein fractionation or isolation

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Summary

Introduction

Proteins are essential to maintain proper energy density of living beings, along with regulating activities of enzymes pertinent to type-2 diabetes, hypertension, and stress relief [1]. Fractionation and/or purification of proteins in the range of 0.1–5 μm could be fractionated by charged UF, peptides around 1–10 μm by membrane chromatography, and that with 0.1–5 nm in size may be gathered by ultrasound (US)-assisted UF, high-performance tangential flow filtration (HPTFF), electro-UF membrane (EUF), electrodialysis with UF membrane (EDUF), and electrodialysis with bipolar membrane (EDBM) [18,19]. The advent of those novel advancements in UF is owing to the bigger challenges in managing the trade-off between productivity and selectivity. Increase from nonhydrolysed dephosphorylated egg-yolk protein, confirmed by [56]

Advancements in Ultrafiltration for Protein and Peptide Separation
Charged-Membrane
Ultrasonic-Assisted UF
Dynamic UF
Integration of UF with Other Processes
Membrane Materials and Molecular Weight Cutoff
Surface Modifications
Ionic Strength
Operating Pressure
Temperature
Findings
Conclusions
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