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2.
Nat Commun ; 14(1): 1026, 2023 Feb 23.
Article in English | MEDLINE | ID: mdl-36823076

ABSTRACT

Dispersion engineering is a powerful and versatile tool that can vary the speed of light signals and induce negative-mass effects in the dynamics of particles and quasiparticles. Here, we show that dissipative coupling between bound electron-hole pairs (excitons) and photons in an optical microcavity can lead to the formation of exciton polaritons with an inverted dispersion of the lower polariton branch and hence, a negative mass. We perform direct measurements of the anomalous dispersion in atomically thin (monolayer) WS2 crystals embedded in planar microcavities and demonstrate that the propagation direction of the negative-mass polaritons is opposite to their momentum. Our study introduces the concept of non-Hermitian dispersion engineering for exciton polaritons and opens a pathway for realising new phases of quantum matter in a solid state.

3.
Bioprocess Biosyst Eng ; 31(3): 163-71, 2008 Apr.
Article in English | MEDLINE | ID: mdl-18239944

ABSTRACT

The immobilization of an endoglucanase, benzoylformate decarboxylase (BFD) from Pseudomonas putida, as well as of lipase B from Candida antarctica (CALB) onto the carrier supports Sepabeads EC-EP, Sepabeads EC-EA, and Sepabeads EC-BU was accomplished. It is shown that via these immobilized biocatalysts the synthesis of both fine and bulk chemicals is possible. This is illustrated by the syntheses of polyglycerol esters and (S)-hydroxy phenyl propanone. The benefit of immobilization is illustrated by repetitive use in a bubble column reactor as well as in a stirred tank reactor. High stability of two biocatalysts was achieved and reusability up to eight times was demonstrated. The comparison of CALB immobilized on Sepabeads EC-EP to Novozym 435 shows similar activity.


Subject(s)
Biotechnology/methods , Enzymes, Immobilized/chemistry , Adsorption , Candida/enzymology , Catalysis , Cellulase/chemistry , Chemistry/methods , Enzymes/chemistry , Escherichia coli/enzymology , Esters/chemistry , Kinetics , Pseudomonas putida/enzymology , Solvents/chemistry , Temperature , Time Factors
5.
Article in German | MEDLINE | ID: mdl-9931912

ABSTRACT

We show that immunohistochemistry for hMSH2 and hMLH1 is an easy and reproducible routine procedure. The interpretation of the staining results is unequivocal and investigator-independent. It is now necessary to validate the specificity and sensitivity of the method in a multicenter study with tumors of known mutations. As a consequence perhaps MIN testing may be replaced by immunohistochemistry as a first-line pretesting for HNPCC, reducing cost and time required.


Subject(s)
DNA-Binding Proteins , Genetic Testing , Neoplasm Proteins/genetics , Proto-Oncogene Proteins/genetics , Adaptor Proteins, Signal Transducing , Adult , Carrier Proteins , Female , Humans , Immunoenzyme Techniques , Male , MutL Protein Homolog 1 , MutS Homolog 2 Protein , Nuclear Proteins , Sensitivity and Specificity
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