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• W2898859622 abstract "In order to address the challenges of relative ratio and relative position among individual enzymes and substrate channeling in multienzyme biocatalysis, we propose a new one-pot genetically encoded self-assembly system as an alternative to the heavy procedure of separately preparing individual enzymes and subsequently co-immobilizing them by physicochemical means, allowing us to construct cell-associated two- or three-enzyme complexes, through the highly specific interaction of cohesin and dockerin domains. Our method for multienzyme complexes (MECs) assembled on Yarrowia lipolytica yeast cells is based on simultaneous surface display of a synthetic multiple cohesins backbone (scaffoldin) and extracellular secretion of dockerin-fusions of individual enzymes. This methodology was applied to fatty acid-derived hydrocarbon (alkenes, alkanes) production. The genetically tailored cell-associated MECs exhibited different proportional and positional effects through genetically encoded customization of the scaffoldin arrangement by varying the copy number and orientation of cohesin domains. The genetically encoded specific positional arrangement of individual enzymes was able to endow MECs with an obvious substrate channeling effect, reflected by a more than 17-fold enhancement in the initial reaction rate. Optimization of the co-immobilized multienzyme complex (through proportional and positional control of cohesin domains) gave much higher conversion yields (71–84%) compared to a free enzymes cocktail (8–32%). The resulting engineered yeast strains, designed for the one-pot fermentation process, integrate surface display of scaffoldin, extracellular production of dockerin-fused individual enzyme components, and highly efficient reassembly of the functional elements through a genetically programmable process. Interestingly, the growing cells of MEC system provides a unique promotion effect to drive the substrate flux toward the final product, through consuming the byproduct (glycerol) as a carbon source during cascade reactions. This adopted technology provides an efficient platform for creating tailored multienzymes for advanced cascade biosynthesis." @default.
• W2898859622 created "2018-11-09" @default.
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• W2898859622 date "2018-10-29" @default.
• W2898859622 modified "2023-10-18" @default.
• W2898859622 title "Design of a New Multienzyme Complex Synthesis System Based on <i>Yarrowia lipolytica</i> Simultaneously Secreted and Surface Displayed Fusion Proteins for Sustainable Production of Fatty Acid-Derived Hydrocarbons" @default.
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• W2898859622 doi "https://doi.org/10.1021/acssuschemeng.8b04401" @default.
• W2898859622 hasPublicationYear "2018" @default.
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