Masarykova Univerzita

Masarykova Univerzita V Brne

Enantis S.r.o.

Zbynek Prokop

Jiri Damborsky

Jan Brezovsky

Yuji Nagata

Radka Chaloupkova

Veronika Stepankova

Pavel Krejci

Lukas Balek

Dick Barend Janssen

Artur Wiktor Gora

Michaela Bosakova

Eva Sebestova

Pavel Vanacek

Livia Eiselleova

David Bednar

Pavel Dvorak

Zaneta Konecna

Petr Dvorak

Tana Koudelakova

Andrea Jesenska

Frantisek Oplustil

Eva Chovancova

Sarka Bidmanova

Axel Dürkop

Otto S Wolfbeis

The invention provides an isolated thermostable polypeptide possessing FGF2 activity and having at least 85% sequence identity to SEQ ID NO: 2 (FGF2 wt) or a functional fragment thereof, and comprising at least one amino acid substitution R31L and the use thereof in the cell biology research, regenerative medicine and related medical applications or cosmetics. Further it discloses a culture medium comprising subjected FGF2 suitable for culturing a human pluripotent stem cells involving both human embryonic stem cells and induced pluripotent stem cells.

Thermostable FGF2 polypeptide, use thereof

Thermostabilization of a protein where the protein contains access routes and wherein at least one amino acid in the bottleneck of the access route is mutated, includes identifying the amino acids of the bottleneck and the amino acids control exchange of the solvent between a buried protein core and surrounding environment and/or in the packing of the amino acids inside the access route. Modification of the amino acids are determined so that the packing of the amino acids inside the tunnel is improved and the access route prevents access of undesired solvent molecules to the protein core, while allowing passage of the compounds necessary at the protein core to enable the protein to perform its biological function.

Method of thermostabilization of a protein and/or stabilization towards organic solvents

The method of detoxification of yperite&#x2014;bis(2-chloroethyl)sulfide&#x2014;by the use of a haloalkane dehalogenases or their compositions, the method of preparation of dehalogenationating enzymes and of decontamination compositions which contains at least one wild type and/or modified haloalkane dehalogenase (EC 3.8.1.5) as an chemically active component. The preferred dehalogenases are LinB fromUT26, DhaA fromNCIMB 13064, DmbA from5033/66. Decontamination is utilizable for detoxification of yperite from the surfaces of instrumentality, constructional objects, human or animal skin and elements of environment by the treatment of yperite with the detoxification composition according the invention at +10&#xb0; C. to +70&#xb0; C., preferably at about +40&#xb0; C. and pH from 4 to 12.

Method of detoxification of yperite by using haloalkane dehalogenases

A method of production of optically active compounds, particularly halohydrocarbons, haloalcohols, alcohols, halopolyols and polyols using hydrolytic dehalogenation of racemic or prochiral halegenhydrocarbons by dehalohenation catalysed by haloalkane dehalogenases (the enzyme code number EC 3.8.1.5) where at least one wild type or modified haloalkane dehalogenase is applied to at least one racemic or prochiral chlorinated, brominated or iodinated compound at the temperature ranged between +10 and +70&#xb0; C. and pH value between 4.0 and 12.0, in aqueous system or in a monophasic organic solution or in a monophasic organic/aqueous solution or in organic/aqueous biphasic systems.

Method of production of optically active halohydrocarbons and alcohols using hydrolytic dehalogenation catalysed by haloalkane dehalogenases

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Brno, Czechia

Zbynek Prokop