Bacterial Inclusion Bodies: A Treasure Trove of Bioactive Proteins. Issue 5 (May 2020)

• Record Type: Journal Article
• Authors: Singhvi, Priyank; Saneja, Ankit; Srichandan, Sudeepa; Panda, Amulya K.
• Is Part Of: Trends in biotechnology. Volume 38:Issue 5(2020)
• Page Start: 474
• Page End: 486
• Publication Date: 2020-05
• Subjects: bacterial inclusion bodies -- mild solubilization agents -- protein purification -- protein refolding -- protein aggregates -- combinatorial approach; Biotechnology -- Periodicals; Biochemical engineering -- Periodicals; Genetic engineering -- Periodicals; Industrial microbiology -- Periodicals; 660.605
• DOI: 10.1016/j.tibtech.2019.12.011
• Languages: English
• ISSNs: 0167-7799

Abstract

Abstract : Recombinant proteins expressed as bacterial inclusion bodies (IBs) are now receiving tremendous attention for many diverse applications in the areas of industrial and medical biotechnology. Understanding the structure–function relationship of protein in IBs has recently created new possibilities in developing innovative isolation, solubilization, refolding, and purification processes for high-throughput recovery of bioactive protein from bacterial IBs. This opinion article describes the advantages, disadvantages, and major challenges presently associated with each of the processing steps. Finally, we conclude with the possible solutions for each operational step and the future direction of the basic and translational research to achieve maximum benefit from IB aggregates. Highlights: In the past decade, considerable attention has been given to developing bioprocess methods that could plausibly decrease the number of operational steps and bring forth a universal strategy for recovering bioactive protein from any bacterial IB. Methods to isolate IBs are developed such that bacterial cells are disrupted effectively while maintaining the integrity of IBs. Novel mild-denaturing solubilization agents based on combinatorial approaches with high solubilization and refolding yield were recently reported. Screening for optimal refolding conditions and methods has become particularly important to ensure a good yield of correctly folded protein. Multimodal chromatography has offered the possibility of purifying the protein at laboratory and industrial scale based on the different protein properties.