Silver nanoparticles (AgNPs) have been found to have extensive biomedical and biological applications. They can be synthesised using chemical and biological methods, and coated by polymer to enhance their stability. Hence, the changes in the physico-chemical characteristics of AgNPs must be scrutinised due to their importance for biological activity. The UV-Visible absorption spectra of polyethylene glycol (PEG) -coated AgNPs displayed a distinctive narrow peak compared to uncoated AgNPs. In addition, High-Resolution Transmission Electron Microscopy analysis revealed that the shapes of all AgNPs, were predominantly spherical, triangular, and rod-shaped. Fourier-Transform Infrared Spectroscopy analysis further confirmed the role of PEG molecules in the reduction and stabilisation of the AgNPs. Moreover, dynamic light scattering analysis also revealed that the polydispersity index values of PEG-coated AgNPs were lower than the uncoated AgNPs, implying a more uniform size distribution. Furthermore, the uncoated and PEG-coated biologically synthesised AgNPs demonstrated antagonisms activities towards tested pathogenic bacteria, whereas no antagonism activity was detected for the chemically synthesised AgNPs. Overall, generalisation on the interrelations of synthesis methods, PEG coating, characteristics, and antimicrobial activity of AgNPs were established in this study.
In a conventional protein downstream processing (DSP) scheme, chromatography is the single most expensive step. Despite being highly effective, it often has a low process throughput due to its semibatch nature, sometimes with nonreproducible results and relatively complex process development. Hence, more work is required to develop alternative purification methods that are more cost-effective, but exhibiting nearly comparable performance. In recent years, surfactant precipitation has been heralded as a promising new method for primary protein recovery that meets these criteria and is a simple and cost-effective method that purifies and concentrates. The method requires the direct addition of a surfactant to a complex solution (e.g. a fermentation broth) containing the protein of interest, where the final surfactant concentration is maintained below its critical micelle concentration (CMC) in order to allow for electrostatic and hydrophobic interactions between the surfactant and the target protein. An insoluble (hydrophobic) protein-surfactant complex is formed and backextraction of the target protein from the precipitate into a new aqueous phase is then carried out using either solvent extraction, or addition of a counter-ionic surfactant. Importantly, as highlighted by past researchers, the recovered proteins maintain their activity and structural integrity, as determined by circular dichroism (CD). In this review, various aspects of surfactant precipitation with respect to its general methodology and process mechanism, system parameters influencing performance, protein recovery, process selectivity and process advantages will be highlighted. Moreover, comparisons will be made to reverse micellar extraction, and the current drawbacks/challenges of surfactant precipitation will also be discussed. Finally, promising directions of future work with this separation technique will be highlighted.
Bacteriocin is an important peptide which can be used as an anti-microbial agent in food. However, simpler and more cost-effective purification methods need to be developed compared to chromatography to enhance its commercial viability. Surfactant precipitation was employed for the first time to purify bacteriocin-like inhibitory substance (BLIS) from a fermentation broth of Pediococcus acidilactici Kp10, and the amount precipitated was investigated as a function of anionic surfactant (AOT) concentration, and pH. Protein recovery from the precipitate was accomplished using solvent extraction, and solvent type, NaCl concentration, and ionic strength of the final solution were optimised. Optimal conditions were; 1.05mM of AOT at pH 4 for precipitation, and acetone extraction (with 1mM NaCl), which resulted in an 86.3% yield, and 53.8 purification factor. This study highlighted the fact that surfactant precipitation can be used as a primary recovery method for BLIS from a complex fermentation broth.
Reversed micellear system (RMS) is an innovative technique used for the isolation, extraction and purification of proteins and enzymes. Studies have demonstrated that RMS is an efficient purification technology for extracting proteins and enzymes from natural plant materials or fermentation broth. Lately, reverse micelles have created wider biological applications and with the ease of scaling up and the possibility for continuous process has made RMS a vital purification technique in various field. In this study, an extensive review of RMS with the current application in biotechnology will be examined. This review provides insights with the fundamental principles, key variables and parameters of RMS. In addition, a comparative study of RMS with other liquid-liquid extraction techniques are included. The present review aims to provide a general overview of RMS by summarising the research works, since the introduction of the technology to current development.