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Cinnamaldehyde (CAD) has a wide range of applications in foods and pharmaceuticals and has recently gained prominence as a potent nematicide in agricultural research owing to its high nematicidal activity. In this study, we developed a whole-cell bioconversion system to CAD using engineered Corynebacterium glutamicum.
Cinnamaldehyde (CAD) has a wide range of applications in foods and pharmaceuticals and has recently gained prominence as a potent nematicide in agricultural research owing to its high nematicidal activity. In this study, we developed a whole-cell bioconversion system to CAD using engineered Corynebacterium glutamicum.
Through adaptive laboratory evolution with a biosensor, we succeeded in engineering Klebsiella oxytoca able to utilize high-concentration xylose (>100 g/L) and developed a cost-competitive and sustainable bioprocess for the production of 2,3-butanediol which is a valuable platform chemical with a wide range of applications in polymers, fuels, and cosmetics.
Through adaptive laboratory evolution with a biosensor, we succeeded in engineering Klebsiella oxytoca able to utilize high-concentration xylose (>100 g/L) and developed a cost-competitive and sustainable bioprocess for the production of 2,3-butanediol which is a valuable platform chemical with a wide range of applications in polymers, fuels, and cosmetics.
In this work, the authors developed new platform for the secretory production of recombinant proteins in Corynebacterium glutamicum. From the secretome analysis of fed-batch culture, the potential signal peptide (Cg1514) was isolated and its usefulness was successfully demonstrated with three protein models. All examined proteins could be produced (up to 1.5 g/L) with high purity (>90 %) in fed-batch cultivation.
In this work, the authors developed new platform for the secretory production of recombinant proteins in Corynebacterium glutamicum. From the secretome analysis of fed-batch culture, the potential signal peptide (Cg1514) was isolated and its usefulness was successfully demonstrated with three protein models. All examined proteins could be produced (up to 1.5 g/L) with high purity (>90 %) in fed-batch cultivation.
A light-driven platform for cofactor-free, whole-cell P450 biocatalysis is described. This novel platform does not require any labor-intensive and time-consuming pretreatments and is applicable to any type of bacterial and human cytochrome P450s. Instead of expensive cofactors, the use of an inexpensive photosensitizer, visible light, and a whole-cell system leads to a cost-effective, scalable, and sustainable process for P450-catalyzed reactions.
A light-driven platform for cofactor-free, whole-cell P450 biocatalysis is described. This novel platform does not require any labor-intensive and time-consuming pretreatments and is applicable to any type of bacterial and human cytochrome P450s. Instead of expensive cofactors, the use of an inexpensive photosensitizer, visible light, and a whole-cell system leads to a cost-effective, scalable, and sustainable process for P450-catalyzed reactions.
Artistic illustration of Cytochrome P450 immobilized on poly(3-hydroxybutyrate). Cytochrome P450 monooxygenase, a powerful and multifunctional enzyme, was successfully immobilized on P(3HB) granules via phasin fusion in Escherichia coli, which could be easily purified by centrifugation after cell disruption. It was also successfully demonstrated that the P450-P(3HB) complex could be a potential platform with highly improved stability and catalytic activity compared to that of non-immobilized P450.
Artistic illustration of Cytochrome P450 immobilized on poly(3-hydroxybutyrate). Cytochrome P450 monooxygenase, a powerful and multifunctional enzyme, was successfully immobilized on P(3HB) granules via phasin fusion in Escherichia coli, which could be easily purified by centrifugation after cell disruption. It was also successfully demonstrated that the P450-P(3HB) complex could be a potential platform with highly improved stability and catalytic activity compared to that of non-immobilized P450.
A simple protein-immobilization method on various substrates, including paper and polyethylene fi lm, was developed using initiated chemical vapor deposition (iCVD) followed by thiol–ene click chemistry. Fluorescent proteins, antibodies and protein scaff olds could be immobilized on various surfaces and showed high activities.
A simple protein-immobilization method on various substrates, including paper and polyethylene fi lm, was developed using initiated chemical vapor deposition (iCVD) followed by thiol–ene click chemistry. Fluorescent proteins, antibodies and protein scaff olds could be immobilized on various surfaces and showed high activities.
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