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Kopac, T. Process-Intensified Recovery of Proteins from Aqueous Media. Encyclopedia. Available online: (accessed on 01 December 2023).
Kopac T. Process-Intensified Recovery of Proteins from Aqueous Media. Encyclopedia. Available at: Accessed December 01, 2023.
Kopac, Turkan. "Process-Intensified Recovery of Proteins from Aqueous Media" Encyclopedia, (accessed December 01, 2023).
Kopac, T.(2022, November 21). Process-Intensified Recovery of Proteins from Aqueous Media. In Encyclopedia.
Kopac, Turkan. "Process-Intensified Recovery of Proteins from Aqueous Media." Encyclopedia. Web. 21 November, 2022.
Process-Intensified Recovery of Proteins from Aqueous Media

Various adsorbent types could be employed for adsorptive separation, wastewater treatment and recovery or removal of various pollutants from aqueous media. Process-intensified recovery or adsorption of proteins from aqueous media was studied via the utilization of novel adsorbents as process intensification (PI) methodology.

process intensification water treatment adsorption protein recovery

1. Introduction

Process intensification (PI) research in chemical engineering applications has attracted considerable interest recently. The applications have led to several innovations in most chemical industries due to the satisfaction of the requirements both in an environmentally friendly manner and in remaining cost competitive. PI is aimed towards substantially smaller, energy-efficient, safer sustainable technological developments, in which the major tools involve the reduction in the amount of equipment via the integration of process steps and functionalities; miniaturization; heat and mass transfer improvements by novel mixing strategies, supplementary energy input, external force fields or improved surface configurations; novel energy and separation techniques; batch to continuous mode process transformations to reduce process volumes; and integrated optimization and control strategies [1][2][3][4][5].
Process-intensifying strategies are usually studied under two main classifications, namely PI equipment and methods [3][5][6][7]. Process-intensifying equipment, also called hardware, mainly involves rotating packed beds, catalytic packings, microreactors, and structured reactors. Various other examples of equipment types are structured packed columns; static mixers; microchannel, spinning disc, loop, oscillatory baffled, spinning tube-in-tube and heat-exchange reactors; and compact heat exchangers. Process-intensifying methods, also referred to as software, involve hybrid separations, such as membrane absorption and absorptive distillation; functional materials, such as ionic liquids; alternative sources of energy, such as ultrasound, microwaves, solar energy and centrifugal fields; and multifunctional reactor systems involving reactive extraction and chromatographic reactors. Combining intensified reactors together with renewable energy sources such as solar energy could provide higher motivation for the achievement of green processing targets. A decrease in material and energy consumption would lead to a direct reduction in capital costs [3][6][7][8].
Ramshaw’s research group initiated PI application by developing a rotating packed bed (RPB) for reactive distillation [3][4][8][9][10][11]. Since then, PI has received considerable appreciation and significance due to its potential for more innovative and viable process design options. Significant developments have been achieved in the field over recent years and have resulted in both successful industrial applications and expanding research interests [5][7][12]. PI has emerged as an integral part of the retrofit design and provided intensified environmental and economical benefits. Significant efforts have been devoted to expressing it better for the satisfaction of the requirements of various industrial sectors, including essentially the manufacturing, energy and chemical sectors [8][13].
Various definitions proposed for PI [1][2][3][6][7][9][10][14][15][16][17][18][19][20][21][22][23][24][25] during the years starting in the early 1980s have been discussed in detail [5]. Although the emerging definitions were quite diverse in nature, they were commonly focused on innovation. The European Roadmap of Process Intensification ERPI [17] presented PI as a set of intensely innovational principles in process as well as equipment design benefiting process and chain efficiency, operational and capital costs, quality, process safety and wastes. Baldea [25] defined PI as chemical engineering developments leading to substantially smaller, energy-efficient, safe, cleaner technologies or those integrating multiple operations into fewer devices. PI is a growing trend in chemical engineering and should satisfy the requirements of markets and shareholders [6][15][26]. As the concept will be evolving continuously, it will involve challenges and requirements until a universal definition is determined [13].

2. Process-Intensified Recovery of Proteins from Aqueous Media

Protein–nanoparticle interactions are important for the investigation of the potential utilization of specific particles in drug delivery systems. The parameters influencing protein–nanoparticle interactions, involving temperature, pH, concentration, particle size, modifier type, cytotoxicity and biocompatibility, need to be explored extensively [5][27][28][29][30][31]. In the following examples, process-intensified recovery or adsorption of proteins from aqueous media was studied via the utilization of novel adsorbents as PI methodology.

2.1. Process Intensification System and Strategy: Novel Adsorbents

Ling and Lyddiatt [32] studied PI for the adsorption system of a dye-ligand and an intracellular protein from bakers’ yeast extract in a fluidized bed for the investigation of the performance of a steel–agarose pellicular adsorbent (UpFront, 51–323 μm). They studied the recovery of glyceraldehyde 3-phosphate dehydrogenase (G3PDH). Kopac et al. [33] investigated the interactions and enhanced adsorption of bovine serum albumin (BSA) protein with double-walled carbon nanotubes (DWNTs). The study involved the investigation of protein adsorption equilibrium and kinetics on DWNTs.
The adsorbent used by Ling and Lyddiatt [32] comprised a stainless steel core (nonporous, 60 μm) coated by a porous agarose layer (20 μm), having an adsorptive coating depth corresponding to 40% of the particle radius and a steel core/agarose volume ratio of 1:3.5. Cibacron Blue 3GA dye was immobilized on the adsorbent particles and tested as an affinity ligand for the selective recovery of the protein from the yeast extract.
DWNTs synthesized via the catalytic chemical vapor deposition (CCVD) method using a MgO-based catalyst were utilized and protein adsorption on carbon nanoparticles was examined by Kopac et al. [33] using a batch technique at optimized process conditions (pH 4, 40 °C) for the highest adsorption efficiency. Interactions of positively charged protein molecules with negatively charged nanotubes were examined to understand the electrokinetic properties.

2.2. Process Intensification Achievements

In the study by Ling and Lyddiatt [32], the adsorbent particle density was increased by incorporating a stainless steel core in agarose. A high throughput was obtained by the high-density adsorbent derivatized with Cibacron Blue 3GA, which minimized the adsorption period and maximized the process efficiency. The process of fluidized bed adsorption was enhanced, allowing sufficient time for the protein molecule to diffuse into the pores of sorbent particles. The matrices designed for the optimization of the solid phase required small particle sizes and increased density in order to have a reduced diffusion path and a high superficial velocity for the improvement of film mass transfer. The dynamic binding capacity was enhanced with an increase in bioload as a result of the enhanced driving force for mass transfer. The process was capable of capturing a target protein molecule without predilution of unclarified feedstock with minimized processing time and maximized process efficiency [32].
In the study by Kopac et al. [33], interactions of positively charged protein molecules with negatively charged nanotubes indicated electrostatic attractions. The maximal protein adsorption capacity of carbon nanoparticles was 1221 mg/g. Thermodynamic parameters indicated an endothermic physisorption process of protein adsorption on DWNTs, exhibiting the largest protein adsorption capacity on DWNT samples in comparison to the single-walled CNTs, multiwalled CNTs or metal oxides [34][35][36]. Using this novel adsorbent significantly intensified the protein adsorption [33].


  1. Charpentier, J.-C. In the frame of globalization and sustainability, process intensification, a path to the future of chemical and process engineering (molecules into money). Chem. Eng. J. 2007, 134, 84–92.
  2. Van Gerven, T.; Stankiewicz, A. Structure, Energy, Synergy, Time—The Fundamentals of Process Intensification. Ind. Eng. Chem. Res. 2009, 48, 2465–2474.
  3. Boodhoo, K.; Harvey, A. (Eds.) Process Intensification for Green Chemistry: Engineering Solutions for Sustainable Chemical Processing, 1st ed.; John Wiley & Sons Ltd.: Hoboken, NJ, USA, 2013.
  4. Keil, F.J. Process intensification. Rev. Chem. Eng. 2017, 34, 135–200.
  5. Kopac, T. Emerging applications of process intensification for enhanced separation and energy efficiency, environmentally friendly sustainable adsorptive separations: A review. Int. J. Energy Res. 2021, 45, 15839–15856.
  6. Stankiewicz, A.I.; Moulijn, J.A. Process Intensification: Transforming Chemical Engineering. Chem. Eng. Prog. 2000, 96, 22–34. Available online: (accessed on 20 April 2022).
  7. Tian, Y.; Demirel, S.E.; Hasan, M.M.F.; Pistikopoulos, E.N. An overview of process systems engineering approaches for process intensification: State of the art. Chem. Eng. Process. Process Intensif. 2018, 133, 160–210.
  8. Sikdar, S.K.; Sengupta, D.; Mukherjee, R. Engineering Methods for Decision Making on Relative Sustainability: Process Simulation Approaches. Meas. Prog. Towards Sustain. 2016, 129–152.
  9. Ramshaw, C.; Arkley, K. Process intensification by miniature mass transfer. Process Engin. 1983, 64, 29–31.
  10. Ramshaw, C. Higee distillation—An example of process intensification. Chem. Eng. 1983, 389, 13–14.
  11. Law, R.; Ramshaw, C.; Reay, D. Process intensification—Overcoming impediments to heat and mass transfer enhancement when solids are present, via the IbD project. Therm. Sci. Eng. Progr. 2017, 1, 53–58.
  12. Babi, D.K.; Cruz, M.S.; Gani, R. Fundamentals of Process Intensification: A Process Systems Engineering View. In Process Intensification in Chemical Engineering; Segovia-Hernandez, J.G., Bonilla-Petriciolet, A., Eds.; Springer International Publishing: Cham, Switzerland, 2016; pp. 7–33.
  13. Kim, Y.-H.; Park, L.K.; Yiacoumi, S.; Tsouris, C. Modular Chemical Process Intensification: A Review. Annu. Rev. Chem. Biomol. Eng. 2017, 8, 359–380.
  14. Cross, W.T.; Ramshaw, C. Process Intensification—Laminar flow—Heat transfer. Chem. Eng. Res. Des. 1986, 64, 293–301.
  15. Tsouris, C.; Porcelli, J.V. Process Intensification—Has its time finally come? Chem. Eng. Progr. 2003, 99, 50–55.
  16. Freund, H.; Sundmacher, K. Towards a methodology for the systematic analysis and design of efficient chemical processes—Part 1: From unit operations to elementary process functions. Chem. Eng. Process. Process Intensif. 2008, 47, 2051–2060.
  17. European Roadmap for Process Intensification (ERPI). Creative Energy—Energy Transition. 2008. Available online: (accessed on 1 February 2022).
  18. Arizmendi-Sánchez, J.; Sharratt, P. Phenomena-based modularisation of chemical process models to approach intensive options. Chem. Eng. J. 2008, 135, 83–94.
  19. Reay, D.; Ramshaw, C.; Harvey, A. Process Intensification: Engineering for Efficiency, Sustainability and Flexibility; Butterworth-Heinemann: Oxford, UK, 2008; ISBN 9780750689410.
  20. Becht, S.; Franke, R.; Geißelmann, A.; Hahn, H. An industrial view of process intensification. Chem. Eng. Process. Process Intensif. 2009, 48, 329–332.
  21. Lutze, P.A.; Dada, E.; Gani, R.M.; Woodley, J. Heterogeneous catalytic distillation—A patent review. Recent. Pat. Chem. Eng. 2010, 3, 208–229.
  22. Lutze, P.; Gani, R.; Woodley, J.M. Process intensification: A perspective on process synthesis. Chem. Eng. Process. Process Intensif. 2010, 49, 547–558.
  23. Ponce-Ortega, J.M.; Al-Thubaiti, M.M.; El-Halwagi, M.M. Process intensification: New understanding and systematic approach. Chem. Eng. Process. Process Intensif. 2012, 53, 63–75.
  24. Portha, J.-F.; Falk, L.; Commenge, J.-M. Local and global process intensification. Chem. Eng. Process. Process Intensif. 2014, 84, 1–13.
  25. Baldea, M. From process integration to process intensification. Comput. Chem. Eng. 2015, 81, 104–114.
  26. Yildirim, O.; Kiss, A.A.; Kenig, E.Y. Dividing wall columns in chemical process industry: A review on current activities. Sep. Purif. Technol. 2011, 80, 403–417.
  27. Xu, X.; Mao, X.; Wang, Y.; Li, D.; Du, Z.; Wu, W.; Jiang, L.; Yang, J.; Li, J. Study on the interaction of graphene oxide-silver nanocomposites with bovine serum albumin and the formation of nanoparticle-protein corona. Int. J. Biol. Macromol. 2018, 116, 492–501.
  28. Mutalik, S.P.; Pandey, A.; Mutalik, S. Nanoarchitectronics: A versatile tool for deciphering nanoparticle interaction with cellular proteins, nucleic acids and phospholipids at biological interfaces. Int. J. Biol. Macromol. 2020, 151, 136–158.
  29. Qiu, C.; Wang, C.; Gong, C.; McClements, D.J.; Jin, Z.; Wang, J. Advances in research on preparation, characterization, interaction with proteins, digestion and delivery systems of starch-based nanoparticles. Int. J. Biol. Macromol. 2020, 152, 117–125.
  30. Raychaudhuri, R.; Pandey, A.; Das, S.; Nannuri, S.H.; Joseph, A.; George, S.D.; Vincent, A.P.; Mutalik, S. Nanoparticle impregnated self-supporting protein gel for enhanced reduction in oxidative stress: A molecular dynamics insight for lactoferrin-polyphenol interaction. Int. J. Biol. Macromol. 2021, 189, 100–113.
  31. Mishra, R.K.; Ahmad, A.; Vyawahare, A.; Alam, P.; Khan, T.H.; Khan, R. Biological effects of formation of protein corona onto nanoparticles. Int. J. Biol. Macromol. 2021, 175, 1–18.
  32. Ling, T.C.; Lyddiatt, A. Process intensification of fluidized bed dye-ligand adsorption of G3PDH from unclarified disrupted yeast: A case study of the performance of a high-density steel—Agarose pellicular adsorbent. Protein Expr. Purif. 2005, 42, 160–165.
  33. Kopac, T.; Bozgeyik, K.; Flahaut, E. Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system. J. Mol. Liq. 2018, 252, 1–8.
  34. Kopac, T.; Bozgeyik, K. Equilibrium, Kinetics, and Thermodynamics of Bovine Serum Albumin Adsorption on Single-Walled Carbon Nanotubes. Chem. Eng. Commun. 2016, 203, 1198–1206.
  35. Bozgeyik, K.; Kopac, T. Adsorption Properties of Arc Produced Multi Walled Carbon Nanotubes for Bovine Serum Albumin. Int. J. Chem. React. Eng. 2016, 14, 549–558.
  36. Bozgeyik, K.; Kopac, T. Adsorption of Bovine Serum Albumin onto Metal Oxides: Adsorption Equilibrium and Kinetics onto Alumina and Zirconia. Int. J. Chem. React. Eng. 2010, 8.
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