Ecker, D. M., Jones, S. D. & Levine, H. L. The therapeutic monoclonal antibody market. MAbs 7, 9–14 (2015).
Google Scholar
Zou, X., Zhang, Q., Lu, H., Lin, D. & Yao, S. Development of a hybrid biomimetic ligand with high selectivity and mild elution for antibody purification. Chem. Eng. J. 368, 678–686 (2019).
Google Scholar
Shukla, A. A., Wolfe, L. S., Mostafa, S. S. & Norman, C. Evolving trends in mAb production processes. Bioeng. Transl. Med. 2, 58–69 (2017).
Google Scholar
Gottschalk, U. Bioseparation in antibody manufacturing: The good, the bad and the ugly. Biotechnol. Prog. 24, 496–503 (2008).
Google Scholar
Elgundi, Z., Reslan, M., Cruz, E., Sifniotis, V. & Kayser, V. The state-of-play and future of antibody therapeutics. Adv. Drug Deliv. Rev. 122, 2–19 (2017).
Google Scholar
O’Kennedy, R., Murphy, C. & Devine, T. Technology advancements in antibody purification. Antibody Technol. J. 6, 17–32 (2016).
Giese, G., Myrold, A., Gorrell, J. & Persson, J. Purification of antibodies by precipitating impurities using Polyethylene Glycol to enable a two chromatography step process. J. Chromatogr., B: Anal. Technol. Biomed. Life Sci. 938, 14–21 (2013).
Google Scholar
Yang, H., Peczulis, P., Inguva, P., Li, X. & Heng, J. Y. Y. Continuous protein crystallisation platform and process: Case of lysozyme. Chem. Eng. Res. Des. 136, 529–535 (2018).
Google Scholar
Chew, K. W., Chia, S. R., Lee, S. Y., Zhu, L. & Show, P. L. Enhanced microalgal protein extraction and purification using sustainable microwave-assisted multiphase partitioning technique. Chem. Eng. J. 367, 1–8 (2019).
Google Scholar
Saxena, A., Tripathi, B. P., Kumar, M. & Shahi, V. K. Membrane-based techniques for the separation and purification of proteins: An overview. Adv. Coll. Interface. Sci. 145, 1–22 (2009).
Google Scholar
Szewczuk-Karpisz, K., Wiśniewska, M., Nowicki, P. & Oleszczuk, P. Influence of protein internal stability on its removal mechanism from aqueous solutions using eco-friendly horsetail herb-based engineered biochar. Chem. Eng. J. 388, 156 (2020).
Wilson, J., Ristic, M., Kirkwood, J., Hargreaves, D. & Newman, J. Predicting the effect of chemical factors on the pH of crystallization trials. Iscience 23, 101219 (2020).
Google Scholar
Brange, J. & Vølund, A. Insulin analogs with improved pharmacokinetic profiles. Adv. Drug Deliv. Rev. 35, 307–335 (1999).
Google Scholar
Yang, M. X. et al. Crystalline monoclonal antibodies for subcutaneous delivery. Proc. Natl. Acad. Sci. USA 100, 6934–6939 (2003).
Google Scholar
Shenoy, B., Wang, Y., Shan, W. & Margolin, A. L. Stability of crystalline proteins. Biotechnol. Bioeng. 73, 358–369 (2001).
Google Scholar
Liu, H. F., Ma, J., Winter, C., & Bayer, R. Recovery and purification process development for monoclonal antibody production. mAbs 2, 480–499 (2010).
Hebel, D., Huber, S., Stanislawski, B. & Hekmat, D. Stirred batch crystallization of a therapeutic antibody fragment. J. Biotechnol. 166, 206–211 (2013).
Google Scholar
Chen, W., Yang, H. & Heng, J. Y. Y. Continuous protein crystallization. in The handbook of continuous crystallization 372–392 (2020).
McPherson, A. & Shlichta, P. Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces. Science 239, 385–387 (1988).
Google Scholar
Hodzhaoglu, F., Kurniawan, F., Mirsky, V. & Nanev, C. Gold nanoparticles induce protein crystallization. Cryst. Res. Technol. 43, 588–593 (2008).
Google Scholar
Curcio, E., Fontananova, E., Di Profio, G. & Drioli, E. Influence of the structural properties of poly(vinylidene fluoride) membranes on the heterogeneous nucleation rate of protein crystals. J. Phys. Chem. B 110, 12438–12445 (2006).
Google Scholar
Georgieva, D. G., Kuil, M. E., Oosterkamp, T. H., Zandbergen, H. W. & Abrahams, J. P. Heterogeneous nucleation of three-dimensional protein nanocrystals. Acta Crystallogr. D Biol. Crystallogr. 63, 564–570 (2007).
Google Scholar
Sugahara, M., Asada, Y., Morikawa, Y., Kageyama, Y. & Kunishima, N. Nucleant-mediated protein crystallization with the application of microporous synthetic zeolites. Acta Crystallogr. D Biol. Crystallogr. 64, 686–695 (2008).
Google Scholar
Sengupta Ghatak, A. & Ghatak, A. Disordered nanowrinkle substrates for inducing crystallization over a wide range of concentration of protein and precipitant. Langmuir 29, 4373–4380 (2013).
Google Scholar
Hemming, S. A. et al. The mechanism of protein crystal growth from lipid layers. J. Mol. Biol. 246, 308–316 (1995).
Google Scholar
Ino, K. et al. Heterogeneous nucleation of protein crystals on fluorinated layered silicate. PLoS ONE 6, e22582 (2011).
Google Scholar
Hekmat, D., Huber, M., Lohse, C., Von Den Eichen, N. & Weuster-Botz, D. Continuous crystallization of proteins in a stirred classified product removal tank with a tubular reactor in bypass. Cryst. Growth Des. 17, 4162–4169 (2017).
Google Scholar
Lazo-Vélez, M. A., Serna-Saldívar, S. O., Rosales-Medina, M. F., Tinoco-Alvear, M. & Briones-García, M. Application of Saccharomyces cerevisiae var. boulardii in food processing: A review. J. Appl. Microbiol. 125, 943–951 (2018).
Google Scholar
Chen, H. et al. High production of valencene in Saccharomyces cerevisiae through metabolic engineering. Microb. Cell Fact. 18, 1–14 (2019).
Faria, C., Borges, N., Rocha, I. & Santos, H. Production of mannosylglycerate in Saccharomyces cerevisiae by metabolic engineering and bioprocess optimization. Microb. Cell Fact. 17, 1–11 (2018).
Lipke, P. N. & Ovalle, R. Cell wall architecture in yeast: New structure and new challenges. J. Bacteriol. 180, 3735–3740 (1998).
Google Scholar
Klis, F. M., Mol, P., Hellingwerf, K. & Brul, S. Dynamics of cell wall structure in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 26, 239–256 (2002).
Google Scholar
Lesage, G. & Bussey, H. Cell wall assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70, 317–343 (2006).
Google Scholar
Silvetti, T., Morandi, S., Hintersteiner, M. & Brasca, M. Use of hen egg white lysozyme in the food industry. in Egg innovations and strategies for improvements 233–242 (Elsevier, 2017).
Maia, N. J. L., Corrêa, J. A. F., Rigotti, R. T., Silva, A. A. & Luciano, F. B. Combination of natural antimicrobials for contamination control in ethanol production. World J. Microbiol. Biotechnol. 35, 1–9 (2019).
Google Scholar
Carrillo, W., García-Ruiz, A., Recio, I. & Moreno-Arribas, M. V. Antibacterial activity of hen egg white lysozyme modified by heat and enzymatic treatments against oenological lactic acid bacteria and acetic acid bacteria. J. Food Prot. 77, 1732–1739 (2014).
Google Scholar
Costa, V., Reis, E., Quintanilha, A. & Moradasferreira, P. Acquisition of ethanol tolerance in Saccharomyces cerevisiae: The key role of the mitochondrial superoxide dismutase. Arch. Biochem. Biophys. 300, 608–614 (1993).
Google Scholar
Lewis, J. G., Learmonth, R. P. & Watson, K. Induction of heat, freezing and salt tolerance by heat and salt shock in Saccharomyces cerevisiae. Microbiology 141, 687–694 (1995).
Google Scholar
Stahl, G., Salem, S. N., Chen, L., Zhao, B. & Farabaugh, P. J. Translational accuracy during exponential, postdiauxic, and stationary growth phases in Saccharomyces cerevisiae. Eukaryot. Cell 3, 331–338 (2004).
Google Scholar
Chayen, N. E. Turning protein crystallisation from an art into a science. Curr. Opin. Struct. Biol. 14, 577–583 (2004).
Google Scholar
McPherson, A. Crystallization of biological macromolecules. (1999).
Liang, M. et al. Cross-linked lysozyme crystal templated synthesis of Au nanoparticles as high-performance recyclable catalysts. Nanotechnology 24, 245601 (2013).
Google Scholar
Wei, H. et al. Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme. Nat. Nanotechnol. 6, 93–97 (2011).
Google Scholar
Wang, W. & Roberts, C. J. Protein aggregation–mechanisms, detection, and control. Int. J. Pharm. 550, 251–268 (2018).
Google Scholar
Wolstenholme, C. H. et al. Aggfluor: fluorogenic toolbox enables direct visualization of the multi-step protein aggregation process in live cells. J. Am. Chem. Soc. 142, 17515–17523 (2020).
Google Scholar
Sheinerman, F. B., Norel, R. & Honig, B. Electrostatic aspects of protein–protein interactions. Curr. Opin. Struct. Biol. 10, 153–159 (2000).
Google Scholar
Zhou, H.-X. & Pang, X. Electrostatic interactions in protein structure, folding, binding, and condensation. Chem. Rev. 118, 1691–1741 (2018).
Google Scholar
Smith, G. R. & Sternberg, M. J. E. Prediction of protein–protein interactions by docking methods. Curr. Opin. Struct. Biol. 12, 28–35 (2002).
Google Scholar
Zheng, X. Y., Shen, Y. H., Wang, X. Y. & Wang, T. S. Effect of pH on uranium (VI) biosorption and biomineralization by Saccharomyces cerevisiae. Chemosphere 203, 109–116 (2018).
Google Scholar
Nascimento, J. M., Oliveira, J. D., Rizzo, A. C. L. & Leite, S. G. F. (2019) Biosorption Cu (II) by the yeast Saccharomyces cerevisiae. Biotechnol. Rep. 21, e00315 (2019).

