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 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 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 microorganism strain comprises a gene coding for a recombinant protein and a mutated gene coding for a host protein that is not a protease. The recombinant protein is secreted during a fermentation and the mutated gene coding for the host protein has been mutated so as to cause reduced expression of the host protein compared to the wild-type gene on which the mutated gene is based.

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: 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: A microorganism strain comprises a gene coding for a recombinant protein and a mutated gene coding for a host protein that is not a protease. The recombinant protein is secreted during a fermentation and the mutated gene coding for the host protein has been mutated so as to cause reduced expression of the host protein compared to the wild-type gene on which the mutated gene is based.

Abstract: Biological decomposition of compounds containing Si-C bands such as PDMS takes place under substantially anaerobic conditions in the presence of an alternative electron acceptor.