Enzyme formulation is the composition and physical presentation of a preparation containing an enzyme and the materials surrounding it. The formulation establishes chemical conditions such as pH, ionic composition, and hydration that influence the persistence of functional protein structure [1]. Protein concentration and interactions with the surrounding medium can also alter the formation of aggregates from unfolded or partially unfolded molecules [2]. Thermal unfolding measurements can characterize changes in protein stability associated with particular solution components or bound ligands [3]. Formulations may present the protein in solution or incorporate it within a structured material that controls its physical environment and release [4]. Composition, physical state, catalytic activity, and stability are therefore complementary properties of an enzyme formulation, linking the molecular condition of the catalyst with the characteristics of the complete preparation [5].
- enzyme preparation
- protein stability
- formulation components
- catalytic activity
References
- Sven Frokjaer; Daniel E. Otzen; Protein drug stability: a formulation challenge. Nat. Rev. Drug Discov. 2005, 4, 298-306, 10.1038/nrd1695.
- Christopher J. Roberts; Therapeutic protein aggregation: mechanisms, design, and control. Trends Biotechnol. 2014, 32, 372-380, 10.1016/j.tibtech.2014.05.005.
- Frank H Niesen; Helena Berglund; Masoud Vedadi; The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2007, 2, 2212-2221, 10.1038/nprot.2007.321.
- Scott D. Putney; Paul A. Burke; Improving protein therapeutics with sustained-release formulations. Nat. Biotechnol. 1998, 16, 153-157, 10.1038/nbt0298-153.
- Madalena Martins; Carla Silva; Artur Cavaco-Paulo. Enzyme stabilization for biotechnological applications; Elsevier: Amsterdam, NX, Netherlands, 2019; pp. 107-131. [CrossRef]