Malvern offers a growing range of systems for protein characterisation. DLS provides a rapid measurement that allows rapid comparison of a number of sample conditions and to indicate the presence of large aggregates and small oligomers or aggregates. SEC-LS allows detailed characterisation of the type of oligomers or aggregates present in samples of therapeutic proteins. The results can be used to demonstrate short-term stability and predict shelf life.īoth SEC-LS and DLS were found to be useful for the rigorous testing required to understand and confirm protein stability under various conditions. 1) were used in studies that examined the effects of pH, temperature and concentration on oligomerisation and aggregation behaviours. Malvern's Zetasizer APS, Zetasizer Nano ZS and Viscotek TDAmax SEC-LS (Fig.
The work described here focused on the use of light scattering techniques to test protein stability under a variety of conditions. Understanding and manipulating protein behaviour is a central element of the associated research and a core company expertise. Novozymes Biopharma develops and manufactures high quality, animal-free and regulatory-compliant recombinant ingredients and technologies to support the development of innovative pharmaceutical products. The work is described in an article 'Tools for evaluating the stability of human recombinant albumins used in human therapeutics'. The teams applied the resolving and detection capabilities of size exclusion chromatography light scattering (SEC-LS) and dynamic light scattering (DLS) offered by Malvern systems to monitor the stability of these Novozymes products. These rAlbumins have been developed and optimised to deliver a safe, stable and regulatory-compliant product for therapeutic formulations. Researchers from Novozymes Biopharma and Malvern Instruments have been collaborating using light scattering techniques to demonstrate the short- and long-term stability of the novel recombinant human albumins Albucult and Recombumin.
Researchers develop methods to test protein stability under a variety of conditions.