Sanofi-A Ventis Deutschland Gmbh

Sanofi

Euroapi

Sebastian Rissom

Thomas Stillger

Hans-Falk Rasser

Rita Bernhardt

Frank Hannemann

Bernd Janocha

Claus Lattemann

Simone Anderko

Andreas Vogel

Claudia Feller

Paul Habermann

Eberhard Ehlers

Frank Zocher

Heinrich Decker

Christophe Salagnad

Reiner Olliger

Laure Landric-Burtin

Guido Seidel

Laure Landric-Burtain

Generally, the present invention relates to the field of steroid hydroxylation. More specifically, the present invention relates to a method for the 21-hydroxylation of steroids in cells. It also relates to cells expressing a steroid 21-hydroxylating enzyme or steroid 21-hydroxylase, expression vectors comprising a nucleic acid encoding for a steroid 21-hydroxylase and a kit for carrying out the method for the 21-hydroxylation of steroids in cells.

21-hydroxylation of steroids

The present invention relates to polypeptide variants of porcine trypsin, to nucleic acid molecules encoding these variants, and to host cells comprising such nucleic acid molecules. It also relates to the use of these variants in methods for producing insulin. The invention further relates to the use of these variants as medicaments, as food ingredients, or as feed ingredients and to the use of these variants within a process of manufacturing a food ingredient or a feed ingredient.

Variants of porcine trypsin

The invention relates to a method for producing C-terminal amidated dibasic or polybasic peptides, consisting in reacting two peptides in the presence of trypsin biologically active enzymes and, if necessary, in purifying the thus obtainable compounds of formula (I) by means of protein chemistry.

Method for amidating polypeptides with basic amino acid C-terminals by means of specific endoproteases

The invention relates to a method for the enzymatic elimination of the N-acyl side chain from lipopeptides to form the corresponding nucleus, wherein the lipopeptide is prepared by fermentation, the lipopeptide being bound to the cells of the biomass, and the biomass is removed with the adhering lipopeptide, the biomass with the adhering lipopeptide is resuspended in an aqueous system, a suitable deacylase is added in dissolved or solid form to the suspension of the biomass, and the corresponding nucleus is formed, and the nucleus is optionally isolated and purified, wherein the lipopeptide obtained by fermentation is reacted after the end of the fermentation as cell-bound biomass without further purification directly with a deacylase, whereby the N-acyl chain linked via an amide linkage is eliminated.

Method for the deacylation of lipopeptides

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Frankfurt am Main, Germany

Sebastian Rissom