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Publication - Professor Adam Perriman

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

    Citation

    Zhou, Y, Jones, N, Pedersen, JN, Perez, B, Hoffmann, S, Petersen, S, Pedersen, J, Perriman, A, Kristensen, P, Gao, R & Guo, Z, 2019, ‘Insight into the structure and activity of surface-engineered lipase biofluids’. ChemBioChem, vol 20., pp. 1266-1272

    Abstract

    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.

    Full details in the University publications repository