Table 1. Main properties of bacterial IBs adjustable through process conditions. Parameter IBs structure features Reference When culture time after induction increased, (Margreiter, et al., IBs median diameter augmented. Also, as the 2008, Upadhyay, culture time passed, IBs showed strong binding et al., 2012, Culture time with Congo red and Thioflavin-T (suggesting Castellanos- more amyloid content), and they became Mendoza, et al., more resistant to proteolysis and 2014) denaturation. Low concentration of inductor (IPTG) (Luo, et al., 2006, Inductor decreased the aggregation and hydrodynamic Margreiter, et al., concentration diameter. Some IBs increased in RP content 2008, Jhamb & under lower inductor concentration. Sahoo, 2012) At low specific growth rates, less abundant IBs (Iafolla, et al., Growth rate were found. However, more RP was present in 2008) IBs formed at the fastest growth rate. (Schein & IBs formed at low temperature presented Noteborn, 1988, some properly folded and active proteins, less Strandberg & impurities, and were solubilized and denatured Enfors, 1991, Temperature faster than those formed at high temperature. Jevsevar, et al., Increase in temperature promoted RP 2005, de Groot & aggregation and improved the IB production Ventura, 2006, rate. Peternel, et al., 2008) (Strandberg & Relative amount of IBs increased with the Enfors, 1991, decline in pH during culture. IBs formed under Castellanos- pH basic pH, presented more -helices, were less Mendoza, et al., resistant to proteolysis and bonded less 2014, Calcines- Thioflavin-T, vs. IBs produced at acidic pH. Cruz, et al., 2018) Diffused protein clusters were seen inside cells cultured in shake flasks under acoustic resonant mixing at high energy (20 g) (Valdez-Cruz, et Agitation compared with IBs formed under orbital al., 2017) agitation. IBs at 20 g were less resistant to proteolysis. 1 Human interferon–α2 (IFN–α2); interferon–γ (IFN–γ); Human growth hormone (hGH); Xylanase (XynB); Alzheimer-related peptide Ab42 mutant fused to green fluorescent protein (Ab42(F19D)-GFP); green fluorescent protein (GFP); protein A from Staphylococcus aureus and I-galactosidase (SpA-gal); Isopropyl β-D-1-thiogalactopyranoside (IPTG); Not determined (N.D.); guanidinium chloride. (GnCl); Thioflavin-T (Th-T); Recombinant protein (RP). 2