Insight into the structure and activity of surface-engineered lipase biofluids

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DOI

Despite a successful application of solvent-free liquid protein (biofluids) concept to a number of commercial enzymes, the technical advantages of enzyme biofluids as hyperthermal stable biocatalysts cannot be fully utilized as up to 90–99% of native activities are lost when enzymes were made into biofluids. With a two-step strategy (site-directed mutagenesis and synthesis of variant biofluids) on Bacillus subtilis lipase A (BsLA), we elucidated a strong dependency of structure and activity on the number and distribution of polymer surfactant binding sites on BsLA surface. Here, it is demonstrated that improved BsLA variants can be engineered via site-mutagenesis by a rational design, either with enhanced activity in aqueous solution in native form, or with improved physical property and increased activity in solvent-free system in the form of a protein liquid. This work answered some fundamental questions about the surface characteristics for construction of biofluids, useful for identifying new strategies for developing advantageous biocatalysts.

Original languageEnglish
JournalChemBioChem
Volume20
Issue10
Pages (from-to)1266-1272
Number of pages7
ISSN1439-4227
DOIs
Publication statusPublished - May 2019

    Research areas

  • lipases, mutagenesis, nanostructures, polymer surfactants, protein engineering, STABILITY, FREE PROTEIN LIQUIDS, BACILLUS-SUBTILIS LIPASE

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