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- W2791285237 abstract "Herein, we report enzyme aggregates assembled around covalently cross-linked streptavidin tetramers. The streptavidin oligomeric matrix (SavMatrix) is produced by using SpyTag/SpyCatch technology and binds tightly to fusion proteins bearing a streptavidin-binding peptide (SBP). Fusing the SBPs to different enzymes leads to precipitation of the streptavidin–enzyme aggregates upon mixing the complementary components. This straightforward strategy can be applied to crude cell-free extracts, allowing the one-step assembly and purification of catalytically active aggregates. Enzyme cascade assemblies can be produced upon adding different SBP-fused enzymes to the SavMatrix. The reaction rate for lactate dehydrogenase (LDH) is improved tenfold (compared with the soluble enzyme) upon precipitation with the SavMatrix from crude cell-free extracts. Additionally, the kinetic parameters are improved. A cascade combining a transaminase with LDH for the synthesis of enantiopure amines from prochiral ketones displays nearly threefold rate enhancement for the synthesis of (R)-α-methylbenzylamine compared with the free enzymes in solution." @default.
- W2791285237 created "2018-03-29" @default.
- W2791285237 creator A5030004908 @default.
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- W2791285237 date "2018-04-26" @default.
- W2791285237 modified "2023-09-24" @default.
- W2791285237 title "Streptavidin-Enzyme Linked Aggregates for the One-Step Assembly and Purification of Enzyme Cascades" @default.
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- W2791285237 doi "https://doi.org/10.1002/cctc.201800162" @default.
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