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Protecting activity of desiccated enzymes
Author(s) -
Piszkiewicz Samantha,
Gunn Kathryn H.,
Warmuth Owen,
Propst Ashlee,
Mehta Aakash,
Nguyen Kenny H.,
Kuhlman Elizabeth,
Guseman Alex J.,
Stadmiller Samantha S.,
Boothby Thomas C.,
Neher Saskia B.,
Pielak Gary J.
Publication year - 2019
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3604
Subject(s) - desiccation , lactate dehydrogenase , desiccation tolerance , enzyme , cytosol , intrinsically disordered proteins , biochemistry , chemistry , dehydrogenase , biology , microbiology and biotechnology , biophysics , botany
Protein‐based biological drugs and many industrial enzymes are unstable, making them prohibitively expensive. Some can be stabilized by formulation with excipients, but most still require low temperature storage. In search of new, more robust excipients, we turned to the tardigrade, a microscopic animal that synthesizes cytosolic abundant heat soluble (CAHS) proteins to protect its cellular components during desiccation. We find that CAHS proteins protect the test enzymes lactate dehydrogenase and lipoprotein lipase against desiccation‐, freezing‐, and lyophilization‐induced deactivation. Our data also show that a variety of globular and disordered protein controls, with no known link to desiccation tolerance, protect our test enzymes. Protection of lactate dehydrogenase correlates, albeit imperfectly, with the charge density of the protein additive, suggesting an approach to tune protection by modifying charge. Our results support the potential use of CAHS proteins as stabilizing excipients in formulations and suggest that other proteins may have similar potential.