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Tjibbe Bosma

Researcher at MorphoSys

Publications -  24
Citations -  1236

Tjibbe Bosma is an academic researcher from MorphoSys. The author has contributed to research in topics: Haloalkane dehalogenase & Phage display. The author has an hindex of 16, co-authored 24 publications receiving 1138 citations. Previous affiliations of Tjibbe Bosma include University of Groningen.

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Halohydrin Dehalogenases Are Structurally and Mechanistically Related to Short-Chain Dehydrogenases/Reductases

TL;DR: A site-directed mutagenesis study, with HheC as a model enzyme, supports a mechanism for halohydrin dehalogenases in which the conserved Tyr145 acts as a catalytic base and Ser132 is involved in substrate binding, since it does not involve a covalent enzyme-substrate intermediate.
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Novel surface display system for proteins on non-genetically modified gram-positive bacteria.

TL;DR: A novel display system is described that allows highly efficient immobilization of heterologous proteins on bacterial surfaces in applications for which the use of genetically modified bacteria is less desirable.
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Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene

TL;DR: The results demonstrated that directed evolution of a key catabolic enzyme and its subsequent recruitment by a suitable host organism can be used for the construction of bacteria for the degradation of a toxic and environmentally recalcitrant chemical.
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Mucosal vaccine delivery of antigens tightly bound to an adjuvant particle made from food-grade bacteria

TL;DR: A non-living and non-genetically modified gram-positive bacterial delivery particle (GEM) that has built-in adjuvant activity and a high loading capacity for externally added heterologous antigens that are fused to a high affinity binding domain is developed.
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A tandem enzyme reaction to produce optically active halohydrins, epoxides and diols

TL;DR: The recombinant halohydrin dehalogenase from Agrobacterium radiobacter AD1 was used to obtain enantiomerically pure halohydrins and epoxides by kinetic resolution and the reversible conversion was drawn to completion.