Abstract: An Escherichia coli bacterial strain contains a gene encoding a recombinant protein and an open reading frame of i) a DNA fragment encoding an N-terminal signal peptide which mediates translocation of the protein into the periplasm, wherein the N-terminal signal peptide is an amino acid sequence with at least 80% correspondence in relation to SEQ ID No. 2 from amino acids 1 to 20 or is a signal peptide of lipoproteins Pal, NlpI, NlpB or OsmB of Escherichia coli, linked to ii) a following DNA sequence (lpp(N)) encoding a lipoprotein (Lpp(N)) which, compared to SEQ ID No. 2 from amino acids 21 to 78, is a different in at most ten amino acids and iii) a further DNA sequence (lpp(C)) encoding a lipoprotein (Lpp(C)) which, compared to SEQ ID No. 2 from amino acids 21 to 78, is a different in at most ten amino acids.

Abstract: The invention relates to a method for producing L-cysteine and its derivatives L-cystine and thiazolidine by fermenting a cysteine-producing microorganism strain in a fermentation medium. The invention is characterized in that L-methionine, L-isoleucine, or L-threonine in respective concentrations ranging from 0.1 to 10 g/L are added to the fermentation medium in the main culture.

Abstract: The invention relates to a method for producing L-cysteine and its derivatives L-cystine and thiazolidine by fermenting a cysteine-producing microorganism strain in a fermentation medium. The invention is characterized in that L-methionine, L-isoleucine, or L-threonine in respective concentrations ranging from 0.1 to 10 g/L are added to the fermentation medium in the main culture.

Abstract: The invention relates to a method for producing L-cystine by fermenting a microorganism strain in a fermentation medium, in which method L-cystine is precipitated in an amount of at least 70% relative to the total cysteine, characterized in that the O2 saturation of the fermentation medium is kept at least at 1% and at most at 40±3% during the formation of L-cystine.

Abstract: A method for the production of natural L-cysteine by fermentation in a production fermenter in which a microorganism strain is cultured in a fermentation medium, characterized in that the fraction of the compounds L-cysteine, L-cystine and thiazolidine in the fermentation medium is controlled in a targeted manner by an iron concentration of a maximum of 8 mg/l in the fermentation medium.

Abstract: A method for the production of natural L-cysteine by fermentation in a production fermenter in which a microorganism strain is cultured in a fermentation medium, characterized in that the fraction of the compounds L-cysteine, L-cystine and thiazolidine in the fermentation medium is controlled in a targeted manner by an iron concentration of a maximum of 8 mg/l in the fermentation medium.

Abstract: The invention relates to a method for producing L-cystine by fermenting a microorganism strain in a fermentation medium, in which method L-cystine is precipitated in an amount of at least 70% relative to the total cysteine, characterized in that the O2 saturation of the fermentation medium is kept at least at 1% and at most at 40±3% during the formation of L-cystine.

Abstract: The present invention relates to a process for producing a correctly folded and assembled full-length antibody using an E. coli strain, which comprises fermenting an E. coli strain which leaks periplasmic proteins into the medium, comprising a gene coding for the heavy chain of an antibody functionally linked to a signal sequence coding for a signal peptide, and a second gene coding for the light chain of an antibody, functionally linked to a signal sequence coding for a signal peptide, in a culture medium, where the E. coli strain secretes a full-length antibody into the culture medium, and the full-length antibody is removed from the culture medium.

Abstract: A process for producing a heterologous protein is provided. The process comprises culturing an E. coli strain in a fermentation medium, the E. coli strain harboring a gene which codes for the heterologous protein and is functionally linked to a signal sequence coding for a signal peptide, and releasing the heterologous protein into the fermentation medium, and the heterologous protein being removed from the fermentation medium, wherein the E. coli strain has an attenuated (p)ppGpp-synthetase II activity (PSII activity).

Abstract: A DNA construct that allows the inexpensive production of a target protein in E. coli, consisting of a nucleic acid sequence encoding a signal peptide which is operably linked with a gene coding for a carrier protein which is linked with a gene coding for the target protein via a gene coding for a cleavable sequence S, wherein the gene coding for a carrier protein is the spy gene from E. coli.

Abstract: A process for producing a heterologous protein is provided. The process comprises culturing an E. coli strain in a fermentation medium, the E. coli strain harboring a gene which codes for the heterologous protein and is functionally linked to a signal sequence coding for a signal peptide, and releasing the heterologous protein into the fermentation medium, and the heterologous protein being removed from the fermentation medium, wherein the E. coli strain has an attenuated (p)ppGpp-synthetase II activity (PSII activity).

Abstract: The present invention relates to a process for producing a heterologous protein by means of an E. coli strain in a fermentation medium. The process comprises fermenting an E. coli strain in a fermentation medium. The E. coli strain has a mutation in the lpp gene or in the promoter region of the lpp gene, and contains a gene coding for a heterologous protein which is functionally linked to a signal sequence coding for a signal peptide. The fermentation medium includes Ca2+ ions in a concentration above 4 mg/l or Mg2+ ions in a concentration above 48 mg/l. The E. coli strain secretes the heterologous protein into the fermentation medium. The protein is removed from the fermentation medium.

Abstract: The present invention relates to a process for producing a correctly folded and assembled full-length antibody using an E. coli strain, which comprises fermenting an E. coli strain which leaks periplasmic proteins into the medium, comprising a gene coding for the heavy chain of an antibody functionally linked to a signal sequence coding for a signal peptide, and a second gene coding for the light chain of an antibody, functionally linked to a signal sequence coding for a signal peptide, in a culture medium, where the E. coli strain secretes a full-length antibody into the culture medium, and the full-length antibody is removed from the culture medium.

Abstract: A DNA construct that allows the inexpensive production of a target protein in E. coli, consisting of a nucleic acid sequence encoding a signal peptide which is operably linked with a gene coding for a carrier protein which is linked with a gene coding for the target protein via a gene coding for a cleavable sequence S, wherein the gene coding for a carrier protein is the spy gene from E. coli.

Abstract: The present invention relates to a process for producing a heterologous protein by means of an E. coli strain in a fermentation medium, in which an E. coli strain which has a mutation in the lpp gene or in the promoter region of the lpp gene, and contains a gene coding for a heterologous protein which is functionally linked to a signal sequence coding for a signal peptide, is fermented on an industrial scale in the fermentation medium, with the E. coli strain secreting the heterologous protein into the fermentation medium, and the protein being removed from the fermentation medium, wherein the heterologous protein comprises more than 70 amino acids.

Abstract: The invention relates to a method for the production of R-?-lipoic acid by fermentation, characterised in that a cell with a weakened lipoyl protein ligase A activity is cultivated in a culture medium, whereby the cell precipitates enantiomerically pure R-?-lipoic acid in the free form in the culture medium and the enantiomerically pure R-?-lipoic acid is separated off from the culture medium.

Abstract: A process is provided for the fermentative preparation of O-acetyl-L-serine. A microorganism strain, which is derived from a wild type and which exhibits an increased endogenous formation of O-acetyl-L-serine and an increased efflux of O-acetyl-L-serine as compared with the wild type, is cultured in a fermentation medium. A pH in the range from 5.1 to 6.5 is set in the fermentation medium.

Abstract: A process is provided for the fermentative preparation of O-acetyl-L-serine. A microorganism strain, which is derived from a wild type and which exhibits an increased endogenous formation of O-acetyl-L-serine and an increased efflux of O-acetyl-L-serine as compared with the wild type, is cultured in a fermentation medium. A pH in the range from 5.1 to 6.5 is set in the fermentation medium.