Cell selected from microorganisms that is able to form at least one rhamnolipid of the general formula, wherein m = 2, 1 or 0, in particular 1 or 0, n = 1 or 0, in particular 1, R 1 and R 2 = independently of one another identical or different organic radical having 2 to 24 carbon atoms, in particular optionally branched, optionally substituted, in particular hydroxy-substituted, optionally unsaturated, in particular optionally mono-, di- or tri-unsaturated, alkyl radical, characterized in that it has been genetically modified such that, compared to its wild type, it has an increased activity of at least one of the enzymes E 1, E 2 and E 3, wherein the enzyme E 1 is able to catalyse the conversion of 3-hydroxyalkanoyl-ACP via 3-hydroxyalkanoyl-3-hydroxyalkanoic acid-ACP to hydroxyalkanoyl-3-hydroxyalkanoic acid, the enzyme E 2 is a rhamnosyltransferase I and is able to catalyse the conversion of dTDP-rhamnose and 3-hydroxyalkanoyl-3-hydroxyalkanoate to α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate and the enzyme E 3 is a rhamnosyltransferase II and is able to catalyse the conversion of dTDP-rhamnose and α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate to α-L-rhamnopyranosyl- -α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate, and characterized in that, compared to its wild type, it has an increased activity of at least one enzyme E 8, which catalyses the export of a rhamnolipid of the general formula from the cell into the surrounding medium, preferably having polypeptide sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28 or having a polypeptide sequence in which up to 25% of the amino acid residues are modified by deletion, insertion, substitution or a combination thereof compared to the respective reference sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28 and which still has at least 10% of the enzymatic activity of the enzyme having the respective reference sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28. m = 2, 1 or 0, in particular 1 or 0, n = 1 or 0, in particular 1, R 1 and R 2 = independently of one another identical or different organic radical having 2 to 24 carbon atoms, in particular optionally branched, optionally substituted, in particular hydroxy-substituted, optionally unsaturated, in particular optionally mono-, di- or tri-unsaturated, alkyl radical, characterized in that it has been genetically modified such that, compared to its wild type, it has an increased activity of at least one of the enzymes E 1, E 2 and E 3, wherein the enzyme E 1 is able to catalyse the conversion of 3-hydroxyalkanoyl-ACP via 3-hydroxyalkanoyl-3-hydroxyalkanoic acid-ACP to hydroxyalkanoyl-3-hydroxyalkanoic acid, the enzyme E 2 is a rhamnosyltransferase I and is able to catalyse the conversion of dTDP-rhamnose and 3-hydroxyalkanoyl-3-hydroxyalkanoate to α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate and the enzyme E 3 is a rhamnosyltransferase II and is able to catalyse the conversion of dTDP-rhamnose and α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate to α-L-rhamnopyranosyl- -α-L-rhamnopyranosyl-3-hydroxyalkanoyl-3-hydroxyalkanoate, and characterized in that, compared to its wild type, it has an increased activity of at least one enzyme E 8, which catalyses the export of a rhamnolipid of the general formula from the cell into the surrounding medium, preferably having polypeptide sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28 or having a polypeptide sequence in which up to 25% of the amino acid residues are modified by deletion, insertion, substitution or a combination thereof compared to the respective reference sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28 and which still has at least 10% of the enzymatic activity of the enzyme having the respective reference sequence Seq ID No. 8, Seq ID No. 24, Seq ID No. 26 or Seq ID No. 28.