Abstract: The invention concerns a polypeptide which can be isolated from the Brassicaceae family and which has at least the activity of a hydroxynitrile lyase (HNL). The hydroxynitrile lyase of the invention is the first HNL from the Brassicaceae family. The plants (Arabidopsis) from which this enzyme or its gene is isolated is also described as non-cyanogenic. All HNL-containing plants described so far are cyanogenic plants and so it has until now been assumed that only cyanogenic plants contain hydroxynitrile lyases. Surprisingly, it transpires that a polypeptide (AtHNL) of the invention is (R)-selective. The amino acid sequence gives a theoretical molecular weight of 29.2 kDa for the AtHNL subunit. The calculated molecular mass of the protein of approximately 30 kDa can be confirmed by SDS gel electrophoresis.
Abstract: The present invention relates to the use of a protein comprising an LOV domain for the photosensitive defunctionalization of a molecule and to a method for the photosensitive defunctionalization of a target molecule.
Type:
Application
Filed:
August 16, 2011
Publication date:
September 5, 2013
Applicant:
EVOCATAL GMBH
Inventors:
Karl Erich Jaeger, Thomas Drepper, Stephan Endres, Janko Potzkei
Abstract: A FRET donor-acceptor pair for use as a biosensor, comprising at least two fluorescence proteins, wherein at least one fluorescence protein is stable with respect to a parameter to be detected by the biosensor and at least one fluorescence protein is unstable with respect to the parameter to be detected by the biosensor.
Type:
Application
Filed:
August 16, 2011
Publication date:
October 24, 2013
Applicant:
EVOCATAL GMBH
Inventors:
Karl Erich Jaeger, Thomas Drepper, Stephan Endres, Janko Potzkei, Achim Heck, Franco Circolone
Abstract: A FRET donor-acceptor pair for use as a biosensor, comprising at least two fluorescence proteins, wherein at least one fluorescence protein is stable with respect to a parameter to be detected by the biosensor and at least one fluorescence protein is unstable with respect to the parameter to be detected by the biosensor.
Type:
Grant
Filed:
August 16, 2011
Date of Patent:
October 7, 2014
Assignee:
Evocatal GmbH
Inventors:
Karl Erich Jaeger, Thomas Drepper, Stephan Endres, Janko Potzkei, Achim Heck, Franco Circolone
Abstract: The present invention provides variants of fluorescent proteins, which are improved with regard to their properties for use as reporter proteins and/or in analytics. In particular, variants of fluorescent proteins are provided, which fluoresce brighter, show improved quantum yield and/or have shifted excitation or emission spectra. The fluorescent proteins according to the invention comprise in their LOV domain besides the substitution of a cysteine with an amino acid that does not covalently bind FMN at least one further point mutation.
Type:
Application
Filed:
May 19, 2010
Publication date:
December 2, 2010
Applicant:
EVOCATAL GMBH
Inventors:
Thorsten Eggert, Sascha Hausmann, Michael Puls
Abstract: The present invention provides variants of fluorescent proteins, which are improved with regard to their properties for use as reporter proteins and/or in analytics. In particular, variants of fluorescent proteins are provided, which fluoresce brighter, show improved quantum yield and/or have shifted excitation or emission spectra. The fluorescent proteins according to the invention comprise in their LOV domain besides the substitution of a cysteine with an amino acid that does not covalently bind FMN at least one further point mutation.
Type:
Grant
Filed:
May 19, 2010
Date of Patent:
September 17, 2013
Assignee:
Evocatal GmbH
Inventors:
Thorsten Eggert, Sascha Hausmann, Michael Puls
Abstract: The invention concerns a polypeptide which can be isolated from the Brassicaceae family and which has at least the activity of a hydroxynitrile lyase (HNL). The hydroxynitrile lyase of the invention is the first HNL from the Brassicaceae family. The plants (Arabidopsis) from which this enzyme or its gene is isolated is also described as non-cyanogenic. All HNL-containing plants described so far are cyanogenic plants and so it has until now been assumed that only cyanogenic plants contain hydroxynitrile lyases. Surprisingly, it transpires that a polypeptide (AtHNL) of the invention is (R)-selective. The amino acid sequence gives a theoretical molecular weight of 29.2 kDa for the AtHNL subunit. The calculated molecular mass of the protein of approximately 30 kDa can be confirmed by SDS gel electrophoresis.
Abstract: To investigate protein-protein interactions, protein foldings and protein localization and also in the secretion of proteins, in vivo reporter proteins are used in biotechnology and in basic research. In order to be able to utilize fluorescence reporters as markers for secretion processes, FMN-binding fluorescence proteins (FbFP) have been developed by us for the first time. The new fluorescence markers can be expressed like GFP in various bacteria. The binding of the chromophore FMN produces a cyan-green fluorescent protein which can be detected in vivo using all customary spectroscopic and microscopic methods. In contrast to GFP, this protein can also surprisingly be secreted via the Sec route and be converted to the fluorescence-active state in the periplasma.
Type:
Application
Filed:
July 27, 2012
Publication date:
August 14, 2014
Applicant:
EVOCATAL GMBH
Inventors:
Thomas Drepper, Karl-Erich Jaeger, Janko Potzkei
Abstract: The invention concerns a polypeptide which can be isolated from the Brassicaceae family and which has at least the activity of a hydroxynitrile lyase (HNL). The hydroxynitrile lyase of the invention is the first HNL from the Brassicaceae family. The plants (Arabidopsis) from which this enzyme or its gene is isolated is also described as non-cyanogenic. All HNL-containing plants described so far are cyanogenic plants and so it has until now been assumed that only cyanogenic plants contain hydroxynitrile lyases. Surprisingly, it transpires that a polypeptide (AtHNL) of the invention is (R)-selective. The amino acid sequence gives a theoretical molecular weight of 29.2 kDa for the AtHNL subunit. The calculated molecular mass of the protein of approximately 30 kDa can be confirmed by SDS gel electrophoresis.