Abstract
This perspective details a robust chemical modification strategy to protect proteins from temperature, aggregation, and non-aqueous environments.
Highlights
Ever since the pioneering work of Klibanov and others to show that enzymes could retain activity in organic solvents,[1,2,3,4] subsequent research focussed on understanding and improving their activity in non-aqueous environments.[5,6,7,8,9,10] The ultimate goal has been – and continues to be – the expansion of the repertoire of enzymes for their use in industrial biocatalysis.[11,12,13,14,15,16,17] The drive behind using enzymes in non-aqueous environments lies in the tantalising prospect of using the vast range and high selectivity and specificity of enzymes with the ubiquity of organic solventsDr Alex P
Solvent-free liquid proteins are a new class of biomaterial with a steadily growing literature base that demonstrates the expanding diversity of proteins, enzymes, and viruses that can form liquids
Proteins in the solvent-free liquid state retain structural dynamics as if they were in water, which results in biological function that is maintained at temperatures far exceeding what is capable under aqueous conditions
Summary
Ever since the pioneering work of Klibanov and others to show that enzymes could retain activity in organic solvents,[1,2,3,4] subsequent research focussed on understanding and improving their activity in non-aqueous environments.[5,6,7,8,9,10] The ultimate goal has been – and continues to be – the expansion of the repertoire of enzymes for their use in industrial biocatalysis.[11,12,13,14,15,16,17] The drive behind using enzymes in non-aqueous environments lies in the tantalising prospect of using the vast range and high selectivity and specificity of enzymes with the ubiquity of organic solventsDr Alex P. Chemical modification of proteins to yield solvent-free liquid proteins has been demonstrated to be a robust method for stabilizing proteins against temperature, aggregation, and non-aqueous environments.
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