Mutated bacterial strains tolerant to elevated concentrations of amines

Abstract

The present invention concerns a novel mutated bacterium tolerant to elevated concentrations of one or more amine compound(s), the mutated bacterium being derived from a reference bacterium by insertion of one or more mutations in its genome, wherein the bacterium is a diderm bacterium and the mutation(s) is(are) present in one or more types of genes or intergenic regions. The invention also relates to in vitro methods using or to in vitro uses of the mutated bacterium of the invention in relation of amine compounds production or transformation.

Description

[0001]MUTATED BACTERIAL STRAINS TOLERANT TO ELEVATED CONCENTRATIONS OF AMINES TECHNICAL FIELD OF THE INVENTION The present invention relates to the fields of microbiology and biocatalysis, and more particularly tothe biotransformation and / or the bioproduction of amine compounds.The present Inventors have indeed developed novel and powerful bacterial strains tolerant to elevated concentrations of amine compounds. The invention therefore notably concerns a mutated bacterium tolerant to elevated concentrations of amine compounds, wherein the bacterium is a diderm bacterium, and wherein the bacterium comprises one mutation or more in its genome. BACKGROUND ART In an international movement of energy transition, biocatalysis which uses enzymes as catalysts of chemical reactions, meets the needs of a more sustainable chemistry (mild conditions, aqueousmedia, chemo-, regio- and stereoselectivity…).In particular, biocatalysis can enable the direct synthesis of enantiopure chiral amines from prochiral ketones mainly through the use of NAD(P)H-dependent enzymes performing reductive amination (Ducrot et al., 2021; Mutti and Knaus, 2021) and ω-transaminases (Slabu et al., 2017). These enzymes can be utilized (free or immobilized) in purified form, in cell-free extracts, or in whole-cells systems. Whole-cell systems are advantageous in terms of increased enzyme stability, direct applicability, andlow preparation cost (Klatte et al., 2014). Indeed, the use of whole cells circumvents the expenses ofcell lysis and enzyme purification whereas the protective nature of the cellular environment stabilizes the biocatalyst (Lin and Tao, 2017). Nonetheless, toxicity of substrates, intermediates, and / or products is a potential drawback when living cells are used. For instance, when assessing the bioamination of alcohols by combining an alcohol dehydrogenase (ADH) with an amine dehydrogenase(AmDH) in vivo, moderate concentrations (less than 20 mM and as little as about 2 mM in some cases)of some amine products were toxic and caused cell death, hence limiting the amine titres to a maximum of about 15 mM for the best converted substrate (Houwman et al., 2019). Therefore, the cellular toxicity of amines is one of the key factors limiting the use of bacterial cells, in particularEscherichia coli (E. coli) cells, as whole-cell catalysts to perform efficient biocatalytic synthesis ofamines. The latter being key compounds in chemical industry together with high value molecules serving as building blocks for the preparation of pharmaceutical and agrochemical active ingredients, this problem has to be solved to enable such biotechnological alternative to become practicable options. Addition of a water immiscible co-solvent, which acts as a reservoir of the toxic compound, can tosome extent alleviate its inhibitory and / or toxicity activity and is used in some applications. However, conventional organic solvents are themselves toxic to the cells while biocompatible solvents are limited and usually more expensive. Accordingly, strategies to physically protect living metabolicallyactive bacterial strain cells (Escherichia coli) for robust biocatalysis have been recently proposed,including—for example—encapsulation by coating the cells with polydopamine (Sun et al., 2022), and cell embedding into alginate hydrogels (Gao et al., 2022). Thus, these solutions are based on amodification of the environment of the cells. However, these approaches are still underdeveloped;particularly, the interactions between cell function and the matrix microenvironment are poorlyunderstood, and additional process costs and limitations for upscaling must be considered.Thus, there is a need to provide novel bacterial strains that are intrinsically more tolerant to elevated concentrations of amine compounds compared to known bacterial strains. However, the mechanisms by which amines interfere with bacterial metabolism are not known, hampering the generation of mutated bacterial strains by conventional means. SUMMARY OF THE INVENTION The present invention fulfils this need. Indeed, the present Inventors have designed novel mutated bacteria tolerant to elevated concentrations of amine compounds. More specifically, the Inventors demonstrate for the first time that mutated bacteria tolerant to elevated concentrations of various amine compounds can be obtained using adaptive evolution protocols. In particular, using the GENEMAT technology for automated continuous culture (WO2000 / 034433) and specific adaptiveevolution steps, the inventors were able to isolate E. coli mutants that tolerate increasedconcentrations of various amine compounds compared to the starting E. coli strain.The data unexpectedly show that, although only one particular amine compound was used in culturemedia, the obtained E. coli mutants tolerate increased concentrations of several other aminecompounds compared to the starting E. coli strain.Therefore, the present invention provides an original, efficient, and easy strategy for selecting bacterial mutants tolerant to elevated concentrations of amine compounds.The present invention thus relates to a mutated bacterium tolerant to elevated concentrations of oneor more amine compound(s), the mutated bacterium being derived from a reference bacterium by insertion of one or more mutations in its genome, wherein the bacterium is a diderm bacterium, and wherein:- at least one mutation occurs in a gene selected from the group consisting of:(i) genes encoding proteins involved in lipid transport and / or lipid metabolism;(ii) genes encoding proteins involved in carbohydrate transport and / or carbohydrate metabolism;(iii) genes encoding proteins involved in nucleotide transport and / or nucleotide metabolism;(iv) genes encoding proteins involved in energy production and / or energy conversion;(v) genes encoding proteins involved in cell cycle control, cell division, chromosome partitioning,and any combination thereof; (vi) genes encoding proteins involved in translation, ribosomal structure ribosomal biogenesis,and any combination thereof; (vii)genes encoding proteins involved in transcription; (viii) genes encoding proteins involved in cell wall biogenesis, cell membrane biogenesis,cell envelope biogenesis, and any combination thereof; (ix) genes encoding proteins involved in intracellular trafficking, secretion, vesicular transport,and any combination thereof; (x) genes encoding proteins involved in signal transduction mechanisms;(xi) genes encoding proteins involved in inorganic ion transport and / or inorganic ion metabolism; (xii) genes encoding proteins involved in ; and(xiii) any combination of (i) to (xii); and / or- at least one mutation occurs in an intergenic region, wherein the intergenic region is preferablyselected from regions involved in the regulation of gene expression, more preferably selected from the group consisting of: (i) the intergenic region located between gene paoA (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00245) and gene yagU (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00246), (ii) the intergenic regions located between gene yfgO (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02385) and gene bepA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02386), (iii) the intergenic regions located between gene rluD (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02484) and gene bamD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02485), and (iv) any combination thereof.The present invention thus also relates to an in vitro use of the mutated bacterium according to theinvention, for the transformation (preferably the biotransformation) of amine compounds, or for the production (preferably the bioproduction) of amine compounds, or any combination thereof; wherein the amine compound is preferably selected from the group consisting of a compound of formula (Formula I);wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, said groups being optionally substituted,with proviso that R1 and R2 are not both H, orb) R1 and R2 form together a saturated or non-saturated ring optionally substituted and / oroptionally fused with another ring,And wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl, said groups beingoptionally substituted.The present invention also relates to an in vitro method for the transformation (preferably thebiotransformation) of amine compounds, or for the production (preferably the bioproduction) of amine compounds, or any combination thereof; comprising using the mutated bacterium according to the invention; wherein the amine compound is preferably selected from the group consisting of a compound of formula (Formula I);wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, said groups being optionally substituted,with proviso that R1 and R2 are not both H, orb) R1 and R2 form together a saturated or non-saturated ring optionally substituted and / oroptionally fused with another ring,And wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl, said groups beingoptionally substituted.DETAILED DESCRIPTION OF THE INVENTION In the context of the present invention, the present Inventors have designed novel mutated bacteria tolerant to elevated concentrations of amine compounds. More specifically, the Inventors demonstrate for the first time that mutated bacteria tolerant to elevated concentrations of various amine compounds can be obtained using adaptive evolution protocols. In particular, using the GENEMAT technology for automated continuous culture (WO2000 / 034433) and specific adaptiveevolution steps, the inventors were able to isolate E. coli mutants that tolerate increasedconcentrations of various amine compounds compared to the starting E. coli strain.The data unexpectedly show that, although only one particular amine compound was used in culturemedia, the obtained E. coli mutants tolerate increased concentrations of several other aminecompounds compared to the starting E. coli strain.Therefore, the present invention provides an original, efficient, and easy strategy for selecting bacterial mutants tolerant to elevated concentrations of amine compounds. DEFINITIONS Unless specifically defined, all technical and scientific terms used herein have the same meaning as commonly understood by a skill artisan in chemistry, biochemistry, cellular biology, molecular biology, and medical sciences.As used herein throughout the entire text, the terms “a” and “an” are used in the sense that theymean “at least one”, “at least a first”, “one or more” or “one or a plurality” of the referencedcompounds or steps, unless the context dictates otherwise.The term “and / or” wherever used herein includes the meaning of “and”, “or” and “all or any othercombination of the elements connected by said term”.The term “about” or “approximately” as used herein means within 10%, preferably within 8%, andmore preferably within 5%, and more preferably within 3%, and more preferably within 1% of a given value or range. As used herein, when used to define products, compositions, cells, uses and methods, the term“comprising” (and any form of comprising, such as “comprise” and “comprises”), “having” (and anyform of having, such as “have” and “has”), “including” (and any form of including, such as “includes”and “include”) or “containing” (and any form of containing, such as “contains” and “contain”) areopen-ended and do not exclude additional, unrecited elements or method steps. Thus, a polypeptide“comprises” an amino acid sequence when the amino acid sequence might be part of the final (and / orwhole) amino acid sequence of the polypeptide. Such a polypeptide can have up to several hundredadditional amino acid residues. “Consisting of” means excluding any other components or steps“Consisting essentially of” means excluding other components or steps of any essential significance(however, other minor / insignificant components or steps are not excluded). In the present disclosure, the terms “comprising”, “consisting of” and “consisting essentially of” may be replaced with each other, if required.As used herein, a “bacterium” refers to a microscopic and prokaryotic organism present in all media.Bacteria are traditionally classified based on their Gram-staining response into gram-positive andgram-negative bacteria. Gram stain (also referred to as “Gram staining” or “Gram’s method”) is abacteriological laboratory technique used to differentiate bacterial species into two large groups (gram-positive and gram-negative) based on the physical properties of their cell walls. “Gram-positivebacteria” are also referred to as “monoderm bacteria” because they have only one membrane, witha thick layer of peptidoglycan that retains a primary stain, crystal violet. “Gram-negative bacteria” are also referred to as “diderm bacteria” because they have two membranes, the outer membrane having a thinner peptidoglycan layer that allows the crystal violet to wash out on addition of ethanol.They are stained pink or red by a counterstain, commonly safranin or fuchsine. Diderm bacteria canbe divided into various classes, including the Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria, Zetaproteobacteria, and Acidithiobacillia. The class ofGammaproteobacteria contains several orders, including the Enterobacterales order, thePseudomonadales order, the Acidiferrobacteraless order, the Aeromonadales order, theAlteromonadales order, the Arenicellales order, the Candidatus Comchoanobacterales order, theCandidatus Competibacterales order, the Candidatus Foliamicales order, the CandidatusPorifericomitales order, the Candidatus Rariloculales order, the Candidatus Spongiifermentumdalesorder, the Candidatus Tethybacterales order, the Cardiobacteriales order, the Cellvibrionales order,the Chromatiales order, the Immundisolibacterales order, the Kangiellales order, the Legionellalesorder, the Methylococcales order, the Moraxellales order, the Nevskiales order, the Oceanospirillalesorder, the Orbales order, the Pasteurellales order, the Salinisphaerales order, the Thiohalobacteralesorder, the Thiohalomonadales order, the Thiohalorhabdales order, the Thiohalospirales order, theThiotrichales order, the Vibrionales order, and the Xanthomonadales order. All of these orderscontain several families.In particular, the Enterobacterales order includes the Bruguierivoracaceae family, the Budviciaceaefamily, the Candidatus Biekeibacteriaceae family, the Enterobacteriaceae family, the Erwiniaceaefamily, the Hafniaceae family, the Morganellaceae family, the Pectobacteriaceae family, theThorselliaceae family, and the Yersiniaceae family. Each family includes several genera. In particular,the Enterobacteriaceae family includes the following genera: Aranicola, Atlantibacter, Averyella,Buttiauxella, Candidatus Arocatia, Candidatus Aschnera, Candidatus Curculioniphilus, Candidatus Cuticobacterium, Candidatus Gillettellia, Candidatus Ischnodemia, Candidatus Ishikawaella, Candidatus Macropleicola, Candidatus Moranella, Candidatus Phlomobacter, Candidatus Profftia, Candidatus Riesia, Candidatus Rohrkolberia, Candidatus Schneideria, Candidatus Stammerula, Cedecea, Citrobacter, Cronobacter, Dryocola, Edaphovirga, Enterobacter, Entomohabitans, Escherichia, Franconibacter, Huaxiibacter, Intestinirhabdus, Jejubacter, Klebsiella, Raoultella, Kluyvera, Kosakonia, Leclercia, Lelliottia, Mangrovibacter, Phytobacter, Plesiomonas, Pluralibacter, Pseudenterobacter, Pseudescherichia, Pseudocitrobacter, Salmonella, Scandinavium, Shigella, Shimwellia, Siccibacter, Silvania, Superficieibacter, Tenebrionibacter, Tenebrionicola, Trabulsiella,and Yokenella. And each genus includes several species. In particular, the Escherichia genus includesthe Escherichia coli species.Similarly, the Pseudomonadales order includes the Candidatus Azotimanducaceae family, theKetobacteraceae family, the Marinobacteraceae family, the Perlucidibacaceae family, thePseudohongiellaceae family, the Pseudomonadaceae family, and the Ventosimonadaceae family. ThePseudomonadaceae family includes the following genera: Atopomonas, Azomonas, Azorhizophilus,Azotobacter, Denitrificimonas, Entomomonas, Halopseudomonas, Mesophilobacter, Permianibacter,Pseudomonas, Stutzerimonas, and Thiopseudomonas. And the Pseudomonas genus includes severalspecies.As used herein, a “mutated bacterium” refers to a bacterium derived from a “reference bacterium”by insertion in its genome of one or more mutations (a “mutation” being defined as a substitution, a deletion or an insertion of one or more consecutive nucleotides). Each mutation may be either silent or non-silent. As used herein a “silent” mutation does not change the phenotype of the bacterium (e.g. tolerance to amine compounds). For example, a nucleotide substitution that does not change the amino acid encoded by a codon in a coding nucleotide sequence will generally not change the phenotype of the bacterium and thus be silent. Conversely, a “non-silent” mutation refers to a mutation that changes the phenotype of the bacterium (e.g. tolerance to amine compounds). For example, a partial or complete deletion of an ORF, the insertion of a heterologous sequence into an ORF or a substitution that results in a non-functional protein being encoded may change the phenotype of the bacterium and will in this case be considered a non-silent mutation. An alteration of a regulatory nucleotide sequence (for instance, a promoter) may also change the phenotype of the bacterium and will in this case be considered a non-silent mutation. As used herein, a bacterium is “tolerant” or “resistant” (both terms are used herein interchangeably) to a compound of interest (e.g. an amine compound) when it is able to grow in the presence of this compound. The level of tolerance or resistance of a bacterium to a compound of interest may be quantified by the “minimum inhibitory concentration (MIC)”, which is the minimal concentration of the compound of interest required to prevent growth of the bacterium. The MIC of a compound of interest required to prevent growth of a bacterium is abbreviated as “MIC (compound of interest, bacterium)”. The higher is the MIC (compound of interest, bacterium) and the higher is the tolerance or resistance of the bacterium to the compound of interest. Alternatively or in combination, the level of tolerance or resistance of a bacterium to a compound of interest may be quantified by the“minimum inhibitory concentration range (MIC range)”, which is the range of minimalconcentrations of the compound of interest required to prevent growth of a bacterium. The MIC rangeof a compound of interest required to prevent growth of a bacterium is abbreviated as “MIC range (compound of interest, bacterium)”. The higher are the values bounding the MIC range (compound of interest, bacterium), the higher is the tolerance or resistance of the bacterium to the compoundof interest. Alternatively or in combination, the level of tolerance or resistance of a bacterium to acompound of interest may be quantified by the “minimum MIC”, which is the lowest concentration close to the minimum concentration of the compound of interest preventing growth of the bacterium. The minimum MIC of a compound of interest required to prevent growth of a bacterium is abbreviated as “minimum MIC (compound of interest, bacterium)”. The higher is the minimum MIC (compound of interest, bacterium), the higher is the tolerance or resistance of the bacterium to the compound of interest. As used herein, a mutated bacterium is “tolerant to elevated concentrations” or “resistant to elevated concentrations” (both expressions are used herein interchangeably) of a compound of interest when it is tolerant or resistant to higher concentrations of the compound of interest than the reference bacterium from which it is derived. In other words, a mutated bacterium is “tolerant to elevated concentrations” of a compound of interest when the MIC (and / or the MIC range; and / or theminimum MIC) (compound of interest, mutated bacterium tolerant to elevated concentrations of thecompound of interest) is higher than the MIC (and / or the MIC range; and / or the minimum MIC) (compound of interest, reference bacterium from which it is derived). A mutated bacterium may notably be “tolerant to elevated concentrations” of a compound of interest when the MIC (compound of interest, mutated bacterium tolerant to elevated concentrations of the compound of interest) is at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 timeshigher, at least 4 times higher, or even at least 5 times higher than the MIC (and / or the MIC range;and / or the minimum MIC) (compound of interest, reference bacterium from which it is derived).A mutated bacterium may also be tolerant to elevated concentrations of a group of compounds sharing a particular chemical group (e.g. amine compounds) when the MICs (and / or the MIC ranges; and / orthe minimum MICs) of several (i.e., two or more, preferably 3 or more, 4 or more, more preferably 5or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) compounds from the group of compounds required to prevent growth of the mutated bacterium are higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICs (and / or the MIC ranges; and / or the minimum MICs) for the reference bacterium from which it is derived.A mutated bacterium is thus tolerant to elevated concentrations of amine compounds when the MICs(and / or the MIC ranges; and / or the minimum MICs) of several (i.e., two or more, preferably 3 ormore, 4 or more, more preferably 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) amine compounds required to prevent growth of the mutated bacterium are higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICs (and / or the MIC ranges; and / or the minimum MICs) for the reference bacterium from which it is derived. As used herein, an “amine compound” refers to an organic derivative of ammonia (NH3) in which one (the amine is then a “primary amine”), two (the amine is then a “secondary amine”), or all three (the amine is then a “tertiary amine”) of the hydrogen atoms attached to nitrogen are replaced by an organic hydrocarbon group, wherein the nitrogen atom is attached to a carbon atom of the organic hydrocarbon group that is not in a carboxyl (-COOH) group. As used herein, an “alkyl” refers to any straight or branched chain or cyclic chain hydrocarbon radical wherein carbon-carbon bonds are simple bonds. A C1-C6alkyl is an alkyl comprising 1 to 6 carbon atoms and encompasses, without being limited to, methyl, ethyl, propyl, isopropyl, cyclopropyl, butyl, isobutyl, tert-butyl, cyclobutyl, pentyl, cyclopentyl, hexyl, and cyclohexyl. The alkyl group may be substituted or unsubstituted.As used herein, “alkenyl” refers to a radical of formula R-C=C-R’ wherein R and R’ are a hydrogenatom or an alkyl. As used herein, a “heteroalkyl” refers to an alkyl wherein the backbone comprises one or several (e.g 2, 3, or 4) heteroatoms preferably selected from O, N and S. Typically, the heteroalkyl comprises at least one moiety -Alk1-X-Alk2-, wherein X is O, NH or S and Alk1 and Alk2 are alkyl radicals. The heteroalkyl can be cyclic or acyclic. As used herein, a “haloalkyl” refers to an alkyl bearing at least one (e.g. 1, 2, 3 or 4) halogen as substituent. The halogen may be F, CI, Br and I, preferably F or CI.As used herein, an “alkoxy” refers to a radical of formula Alk-O- wherein Alk represents an alkylgroup. As used herein, an “aryl” refers to an aromatic ring system which has 5-14 ring atoms and at least one aromatic ring having a conjugated pi electron system. An aryl may contain more than one aromatic ring such as fused ring systems or an aryl group substituted with another aryl group. Aryl encompasses, without being limited to, phenyl, anthracyl, naphtyl, and biphenyl. An aryl may be substituted or unsubstituted. A preferred aryl group is phenyl optionally substituted.As used herein, an “aryloxy” refers to a radical of formula Ar-O- wherein Ar represents an aryl group.As used herein, an “aryloxyalkyl” refers to a radical of formula Ar-O-Alk- wherein Ar represents anaryl group and Alk represents an alkyl group.As used herein, an “alkyloxyalkyl” refers to a radical of formula Alk1-O-Alk2- wherein each Alk1 andAlk2 are independently selected from alkyls. Alkyloxyalkyl is an example of heteroalkyl radicals.As used herein, an “alkanoylalkyl” refers to a radical of formula Alk1-(C=O)-Alk2- wherein each Alk1and Alk2 are independently selected from alkyls.As used herein, “heteroaryl group” refers to a chemical group having 5-14 ring atoms wherein 1 to 4(e.g.1, 2, 3 or4) heteroatoms are ring atoms in the aromatic ring and the remainder of the ring atoms are carbon atoms. Suitable heteroatoms include oxygen, sulfur, nitrogen, and selenium. Heteroaryl groups include, without being limited to, furanyl, thienyl, pyridyl, pyrrolyl, N-alkyl pyrrolyl, pyridyl- N-oxide, pyrimidyl, pyrazinyl, imidazolyl, benzimidazolyl, benzofuranyl, benzothiophenyl, quinazolinyl, quinolinyl, and the like. The heteroaryl group may be substituted or unsubstituted. A preferred heteroaryl group is pyridyl, optionally substituted.As used herein, a “heteroaryloxy alkyl” refers to a radical of formula Het-O-Alk- wherein Hetrepresents a heteroaryl group and Alk represents an alkyl.As used herein, an “aryl alkyl” refers to a radical of formula Ar-Alk- wherein Ar is an aryl group andAlk is an alkyl. An example of aryl alkyl is Ph-(CH2)P – wherein Ph is a substituted or unsubstitutedphenyl and p is an integer from 1 to 6.As used herein, a “heteroaryl alkyl” refers to a radical of formula HetAr-Alk- wherein HetAr is aheteroaryl group and Alk is an alkyl. As used herein, a “substituted group” refers to a group substituted by one or several substituents, typically 1, 2, 3, 4, 5 or 6 substituents. For instance, the substituents may be independently selected from C1-C6alkyl, aryl group, C3-C6cycloalkyl, C2-C6heterocycloalkyl, C1-C6alkoxy, C1-C6alkylamino, C1-C6 aminoalkyl, C1-C6 Ν,Ν-dialkylamino alkyl, C1-C6 N-alkylamino alkyl, -N3, -NH2, -F, -I, -Br, -OH, - CI, -SH, C1-C6alkanoyl, C1-C6acylamino, -CONH2, -NO2, , OP(=O)(OH)2, -SO3H, C1-C6hydroxyalkyl, C1- C6haloalkyl, C1-C6alkylthio, C2-C10alkoxy alkyl, C2-C6alkoxy carbonyloxy, -CN, -CF3, -COOH, -C(=O)- R, -NHC(=O)R, -C(=O)NHR, SC(=O)R, -C(=O)SR, -OC(=O)R, and -C(=O)OR, wherein R is a C1-C6alkyl. In particular, the substituent(s) may be selected among halogens, in particular F or CI, -OH, C1-C6alkoxy, C1-C6 alkyl, C1-C6 hydroxyalkyl, and C1-C6 halogenoalkyl. When present, a COOH substituent ispreferably at a position other than at a position γ of the carbonyl group, and even at a position otherthan at position α, β, and γ of the carbonyl group.The wording "optionally substituted” can be replaced by the wording “substituted or unsubstituted”throughout this application. As used herein, an “oxo” substituent refers to the presence of a substituent of formula –(=O)-. For instance, as used herein, a cyclohexane substituted with an oxo group refers to cyclohexanone.The terms “peptide”, “polypeptide” and “protein” are used interchangeably herein and refer to anypolymer of covalently linked amino acids, regardless of length or post-translational modification. No limitation is placed on the maximum number of amino acids comprised in a polypeptide. As a general indication, the terms refer to both short polymers (typically designated in the art as peptide, or protein fragment) and longer polymers (typically designated in the art as polypeptide or protein). As a general indication and without being bound therein, if the amino acid polymer contains more than50 amino acid residues, it is preferably referred to as a polypeptide or a protein, whereas if thepolymer consists of 50 or fewer amino acids, it is preferably referred to as a “peptide”. A polypeptidemay be any translational product of a polynucleotide regardless of size. Alternatively, a polypeptide may be any product of a chemical synthesis reaction. The polymer can be linear, branched or cyclic, preferably linear. The polymer may comprise naturally occurring amino acids and / or amino acid analogues and it may be interrupted by non-amino acids. Amino acids in a polypeptide are typically covalently linked by peptide bonds. Preferably, all the chemical bonds in a polypeptide are peptide bonds. Peptide bonds are formed between the carboxyl group of one amino acid and the amino groupof the next amino acid. The terms also apply to amino acid polymers in which one or more aminoacids are chemical analogues or modified derivatives of corresponding naturally occurring aminoacids. In some instances, the polypeptide may comprise one or more chemical bonds which are notpeptide bonds. The term “polypeptide” encompasses native polypeptides, as well as modified non- native polypeptides, including derivatives, mutated polypeptides, engineered polypeptides, fusion polypeptides, among others. The term “polypeptide” also encompasses polypeptide fragments andpolypeptide multimers (e.g. dimers), including homo- and hetero-multimers. Polypeptides usableherein can be further modified by chemical or enzymatic modification. Such a chemically and / or enzymatically modified polypeptide comprises chemical groups other than the chemical groups of the 20 naturally occurring amino acids. Examples of such chemical or enzymatic modifications include post-translational modifications, addition of a label, etc. Chemical or enzymatic modifications of a polypeptide may alter one or more property(ies) of the polypeptide. For example, some modifications may alter stability, biological half-life, water solubility, activity, etc. The reading and writing senses of an amino acid sequence of a polypeptide as used herein are the conventional reading and writing senses. The reading and writing convention for amino acid sequences of a polypeptide places the amino terminus on the left, with the sequence then being written and read from the amino terminus (N-terminus) to the carboxyl terminus (C-terminus), from left to right. Proteins and genes encoding them may be classified in several families depending on their function.In particular, version 5 (v5) of EggNOG (for “Evolutionary genealogy of genes: Non-supervisedOrthologous Groups”) is a public database of orthology relationships, gene evolutionary histories and functional annotations, in which thousands of genomes are analyzed at once to establish orthology relationships between all their genes. In eggnog v5, genomes analysis has been done in various subgroups of organisms (narrow subgroups containing only organisms of the same species or genus, or broader subgroups containing organisms of the same family, order…). Proteins / genes of an Orthologous group (OG, which is a group of orthologous genes) are classified into one or more of 20 functional categories (plus a 21thcategory for poorly characterized protein / genes with unknownfunction) depending on their known or putative function, as described in Table 1 below:Table 1. EggNOG v5 functional categories: EggNOG v5 Category Description of category DCell cycle control, cell division, chromosome partitioningM Cell wall / membrane / envelope biogenesisN Cell motilityO Posttranslational modification, protein turnover, chaperonesT Signal transduction mechanismsU Intracellular trafficking, secretion, and vesicular transportV Defense mechanismsW Extracellular structuresA RNA processing and modificationJ Translation, ribosomal structure and biogenesisK TranscriptionL Replication, recombination and repairC Energy production and conversionE Amino acid transport and metabolismF Nucleotide transport and metabolismG Carbohydrate transport and metabolismH Coenzyme transport and metabolismI Lipid transport and metabolismP Inorganic ion transport and metabolismQ Secondary metabolites biosynthesis, transport and catabolismS Function unknownSome genes may belong to several of the above functional categories. The EggNOG v5 category(ies) to which any gene of interest belongs can be checked in EggNOG v5 database. A protein / gene is said to be “involved in” one of the above categories if this category is mentioned as its category (or oneof its categories) in EggNOG v5 for the genus Escherichia. For example, a protein / gene is said to be“involved in energy production and conversion” if category C is mentioned in EggNOG v5 for the genusEscherichia. A “known function” refers to a function that has been demonstrated experimentally, while a “putative function” refers to a function that is probable in view of sequence or 3D-structure similarity with another protein with a known function. As used herein, “orthologous genes” are genes in different species that evolved from a common ancestor by speciation. Normally, orthologous genes retain the same function in the course of evolution. As used herein, a “gene” refers to a sequence of nucleotides in DNA, that is transcribed to produce a functional RNA. As used herein, an “intergenic region” refers to a stretch of DNA sequence located between two successive genes. Intergenic regions may contain functional elements (such as promoters, enhancers, spacers, origins of replication…) or junk DNA.As used herein, “identity” or “sequence identity” means an exact sequence match between twopolypeptides or amino acids, or between two nucleic acid molecules or oligonucleotides. The “percent identities” referred to in the context of the disclosure of the present invention are determined after optimal alignment of the sequences to be compared, which optimal global alignment may therefore comprise one or more insertions, deletions, truncations and / or substitutions. The alignment is “global”, meaning that it includes the sequences to be compared taken in their entirety over their entire length. The alignment is “optimal”, meaning that the number of insertions, deletions, truncations and / or substitutions is made as low as possible. The optimal global alignmentmay be performed and the percent identity may be calculated using any sequence analysis methodwell-known to the person skilled in the art. In addition to manual comparison, it is possible to determine global alignment using the algorithm of Needleman and Wunsch (A general method applicable to the search for similarities in the amino acid sequence of two proteins, J. Mol. Biol.,1970, Mar;48(3):443-453). The optimal global alignment may be performed and the percent identitymay be calculated using any software well–known to a person skilled in the art, such as the Emboss Needle software. The Emboss Needle software, for example, is available on the ebi.ac.uk world wide website under the name “Align”. This software reads two input sequences and writes their optimal global sequence alignment to file. It uses the Needleman-Wunsch alignment algorithm to find the optimum alignment (including gaps) of two sequences along their entire length. The algorithm uses a dynamic programming method to ensure the alignment is optimum, by exploring all possible alignments and choosing the best. A scoring matrix is read that contains values for every possible residue or nucleotide match. Emboss Needle software finds the alignment with the maximum possible score where the score of an alignment is equal to the sum of the matches taken from the scoring matrix, minus penalties arising from opening and extending gaps in the aligned sequences. The substitution matrix and gap opening and extension penalties are user-specified. In the context of the invention, in order to obtain an optimal global alignment, the Emboss Needle software may be used with default parameters. For nucleotide sequences, the parameters used may notably be the following: “Gap open” equal to 10.0, “Gap extend” equal to 0.5, and the EDNAFULL matrix (NCBI EMBOSS Version NUC4.4). For amino acid sequences, the parameters used may notably be the following: “Gap open” equal to 10.0, “Gap extend” equal to 0.5, and the BLOSUM62 matrix; or theparameters used may be : the “Gap open” parameter equal to 10.0, the “Gap extend” parameterequal to 0.5, the “End gap penalty” parameter to “false”, the “End gap open” parameter to 10.0,and a “Blosum 62” matrix.When entering two amino acid sequences or two nucleotide sequences, the Emboss Needle software returns an optimal global alignment, as well as several values characterizing the alignment: ^“Identity” is the percentage of identity, i.e. the percentage of identical matches betweenthe two sequences over the reported aligned region (including any gaps in the length), ^“Similarity” is the percentage of similarity, i.e. the percentage taking into account both theidentical matches between the two sequences over the reported aligned region (including any gaps in the length), and conservative substitutions. ^“Score” is the total score of the alignment, corresponding to the best score obtained by thesoftware for all tested global alignments (i.e. over the entire length of both sequences). This score may be referred to as a “similarity score”, since the higher is the value of the score between the two (or more) sequences to align, the higher is the similarity between these two (or more) sequences, taking into account not only aligned identical amino acids, but also conservative substitutions. This score may be calculated using any software well–known to a person skilled in the art, such as the Emboss Needle software, and may also be calculated manually. Preferably, the percent identity as defined in the context of the present invention is determined viathe global alignment of sequences compared over their entire length. For illustrative purposes, “atleast 80% identity” herein means any percentage of identity (whether integer or decimal) from 80% to 100%, including 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity. An “identical match” between two (or more) residues (such as amino acid or nucleic acid residues) herein means that the two residues are identical. As used herein, a position X1 in a first nucleic acid sequence or amino acid sequence (for instance a genomic sequence or amino acid sequence of the mutated bacterium of the invention) is “equivalent” to a position X2 in a second nucleic acid sequence or amino acid sequence (for instance a genomicsequence or amino acid sequence of a reference bacterium, such as E. coli strain BL21(DE3)) when,after optimal global alignment of the two nucleic acid sequences (for instance the genome of themutated bacterium of the invention and the genome of the reference bacterium, such as E. coli strainBL21(DE3)), or of the two amino acid sequences (for instance the amino acid sequences of the sameprotein of the mutated bacterium of the invention and the reference bacterium, such as E. coli strainBL21(DE3)), the positions X1 and X2 are aligned in the optimal global alignment of the two nucleic acid sequences.Herein, all Genbank accession numbers refer to Genbank release 258 of October 15, 2023.As used herein, “continuous culture” is a type of bacterial culture technique in which bacterialgrowth is maintained at an exponential phase under strictly controlled conditions. Continuous culturemay be used as a method for directed evolution of microorganisms. Continuous culture of bacteriamay be performed using turbidostat, chemostat, or medium swap culture regime.As used herein, “chemostat” refers to a type of continuous culture system in which the growth of the cell population is fixed by a constant dilution rate of the culture. The growth medium contains one essential nutrient in limiting amounts, mutant cells are selected for higher growth yield. It is an open culture system and has a continuous feed of fresh nutrients at a constant rate. Continuous removal of culture at a constant rate from the other side keeps the volume inside constant. The name‘Chemostat’ implies that the growth rate of the chemostat can be controlled by a single componentof the culture medium inside the culture recipient. The skilled person knows the culture conditionsdepending on the bacterium species. As used herein “turbidostat” refers to a type of continuous culture system in which the culture biomass is maintained constant by measuring the optical density of the culture medium using aphotometer. When turbidity comes to a certain level, a volume of fresh medium is added and adjuststhe turbidity to the required level. Concomitantly, the same volume of the culture is discarded keeping the culture volume constant. Contrary to chemostat, another type of continuous culture system, the growth rate of the microbes does not depend on a single component of the culturemedium, and the flow rate does not remain constant in turbidostat. Thus, a turbidostat can be usedto select mutant cells exhibiting maximized growth rate, in a cell population. As used herein “medium swap” or “medium swap regime” refers to a type of continuous culture system using at least two distinct media, comprising a permissive medium and a stressing medium. The growing culture can be diluted by either permissive or stressing medium. The choice between the two dilution media depends on the turbidity of the culture with respect to a set optical density(OD) threshold (threshold (e.g., OD at 600 nm value of 0.4, preferably an OD at 600 nm value of 0.5,preferably an OD at 600 nm value of 0.6, more preferably OD at 600 nm value of 0.7). When theOD600 nm exceeds the threshold, a defined volume of stressing medium is added (e.g., injected) in theculture system; otherwise, a defined volume of permissive medium is added (e.g., injected) in theculture system. Dilutions are usually triggered every 5-15 minutes (preferably every 10 minutes). Thisregime enables gradual adaptation of a bacterial population to grow in a non-permissive or stressing medium. As used herein, a "permissive medium” is a culture medium comprising (having / containing) a permissive concentration (Cp) of an amine compound. A permissive concentration Cp of an amine compound is preferably equal to its minimum inhibitory concentration (MIC) for the referencebacterium minus 10-20% (MIC-10-20%). A “stressing medium” herein refers to a culture mediumcomprising (having / containing) a stressing concentration (Cs) of amine compound, wherein the Cs ispreferably equal to 1.2xCp (1.2 times Cp), preferably 1.5xCp, more preferably 2xCp, more preferablyat least 2xCp (or wherein the Cs is preferably about 1.2xCp, preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp). As used herein, “transformation of amine compounds” refers to a process in which amine compounds are transformed into one or more other types of chemical compounds. “Biotransformation” refers to transformation in cellulo (by microorganisms) or in vitro (by enzymes). As used herein, “production of amine compounds” refers to a process in which chemical compounds other than amine compounds are transformed into amine compounds. “Bioproduction” refers to production in cellulo (by microorganisms) or in vitro (by enzymes). In the detailed description which follows, the embodiments may be taken alone or combined appropriately by those skilled in the art. MUTATED BACTERIUM In the context of the present invention, the Inventors have selected new mutated bacteria tolerant to elevated concentrations of amine compounds.The present invention thus concerns a mutated bacterium tolerant to elevated concentrations of oneor more amine compound(s), the mutated bacterium being derived from a reference bacterium by insertion of one or more mutations in its genome, wherein the bacterium is a diderm bacterium, and wherein:- at least one mutation occurs in a gene selected from the group consisting of:(i) genes encoding proteins involved in lipid transport and / or lipid metabolism;(ii) genes encoding proteins involved in carbohydrate transport and / or carbohydrate metabolism;(iii) genes encoding proteins involved in nucleotide transport and / or nucleotide metabolism;(iv) genes encoding proteins involved in energy production and / or energy conversion;(v) genes encoding proteins involved in cell cycle control, cell division, chromosome partitioning,and any combination thereof; (vi) genes encoding proteins involved in translation, ribosomal structure ribosomal biogenesis,and any combination thereof; (vii)genes encoding proteins involved in transcription; (viii) genes encoding proteins involved in cell wall biogenesis, cell membrane biogenesis,cell envelope biogenesis, and any combination thereof; (ix) genes encoding proteins involved in intracellular trafficking, secretion, vesicular transport,and any combination thereof; (x) genes encoding proteins involved in signal transduction mechanisms;(xi) genes encoding proteins involved in inorganic ion transport and / or inorganic ion metabolism;(xii) the gene yjgL (GenBank identification number for Escherichia coli strain BL21(DE3):CP001509.3, locus tag : ECD_04119); (xiii) the gene yqjA (GenBank identification number for Escherichia coli strain BL21(DE3) :CP001509.3, locus tag : ECD_02964); and (xiv) any combination of (i) to (xiii); and / or- at least one mutation occurs in an intergenic region, wherein the intergenic region is preferablyselected from regions involved in the regulation of gene expression, more preferably selected from the group consisting of: (i) the intergenic region located between gene paoA (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00245) and gene yagU (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00246), (ii) the intergenic regions located between gene yfgO (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02385) and gene bepA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02386), (iii) the intergenic regions located between gene rluD (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02484) and gene bamD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02485), and(iv) any combination thereof.TYPE OF MUTATED DIDERM BACTERIUMThe mutated diderm bacterium preferably belongs to the Gammaproteobacteria class. Preferably,the mutated diderm bacterium belonging to the Gammaproteobacteria class is derived from areference bacterium belonging to the Gammaproteobacteria class by insertion in its genome of oneor more mutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Gammaproteobacteria class, the mutated diderm bacterium preferably belongs to an orderselected from the group consisting of: -the Enterobacterales order,- the Pseudomonadales order,- the Acidiferrobacteraless order,- the Aeromonadales order,- the Alteromonadales order,- the Arenicellales order,- the Candidatus Comchoanobacterales order,- the Candidatus Competibacterales order,- the Candidatus Foliamicales order,- the Candidatus Porifericomitales order,- the Candidatus Rariloculales order,- the Candidatus Spongiifermentumdales order,- the Candidatus Tethybacterales order,- the Cardiobacteriales order,- the Cellvibrionales order,- the Chromatiales order,- the Immundisolibacterales order,- the Kangiellales order,- the Legionellales order,- the Methylococcales order,- the Moraxellales order,- the Nevskiales order,- the Oceanospirillales order,- the Orbales order,- the Pasteurellales order,- the Salinisphaerales order,- the Thiohalobacterales order- the Thiohalomonadales order- the Thiohalorhabdales order- the Thiohalospirales order- the Thiotrichales order,- the Vibrionales order, and- the Xanthomonadales order.Preferably, the mutated diderm bacterium belonging to one of the above orders is derived from a reference bacterium from the same order by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations.In a preferred embodiment, the mutated diderm bacterium belongs to the Enterobacterales order.Preferably, the mutated diderm bacterium belonging to the Enterobacterales order is derived from areference bacterium from the Enterobacterales order by insertion in its genome of one or moremutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Enterobacterales order, the mutated diderm bacterium preferably belongs to a familyselected from the group consisting of: the Bruguierivoracaceae family, the Budviciaceae family, theCandidatus Biekeibacteriaceae family, the Enterobacteriaceae family, the Erwiniaceae family, theHafniaceae family, the Morganellaceae family, the Pectobacteriaceae family, the Thorselliaceaefamily, and the Yersiniaceae family; more preferably the diderm bacterium belongs to theEnterobacteriaceae family.Preferably, the mutated diderm bacterium belonging to one of the above families is derived from a reference bacterium from the same family by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Enterobacteriaceae family, the mutated diderm bacterium is even more preferably of agenera selected from the group consisting of : Aranicola, Atlantibacter, Averyella, Buttiauxella, Candidatus Arocatia, Candidatus Aschnera, Candidatus Curculioniphilus, Candidatus Cuticobacterium, Candidatus Gillettellia, Candidatus Ischnodemia, Candidatus Ishikawaella, Candidatus Macropleicola, Candidatus Moranella, Candidatus Phlomobacter, Candidatus Profftia, Candidatus Riesia, Candidatus Rohrkolberia, Candidatus Schneideria, Candidatus Stammerula, Cedecea, Citrobacter, Cronobacter, Dryocola, Edaphovirga, Enterobacter, Entomohabitans, Escherichia, Franconibacter, Huaxiibacter, Intestinirhabdus, Jejubacter, Klebsiella, Raoultella, Kluyvera, Kosakonia, Leclercia, Lelliottia, Mangrovibacter, Phytobacter, Plesiomonas, Pluralibacter, Pseudenterobacter, Pseudescherichia, Pseudocitrobacter, Salmonella, Scandinavium, Shigella, Shimwellia, Siccibacter, Silvania, Superficieibacter, Tenebrionibacter, Tenebrionicola, Trabulsiella,and Yokenella; even more preferably the mutated diderm bacterium belongs to the Escherichia genus.Preferably, the mutated diderm bacterium belonging to one of the above genera is derived from a reference bacterium from the same genus by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Escherichia genus, the mutated diderm bacterium preferably belongs to Escherichia coli(abbreviated as “E. coli”) species.Preferably, the mutated diderm bacterium belonging to E. coli species is derived from a referencebacterium from E. coli species by insertion in its genome of one or more mutations, preferably byinsertion in its genome of one or more non-silent mutations. Within the Escherichia coli species, the mutated diderm bacterium is preferably derived from areference Escherichia coli strain selected from Escherichia coli strain BL21(DE3: Derivative of E. coli),HMS174(DE3) (K12-derivative), and MG1655.Information regarding public availability of the above-mentioned E. coli strains is provided in Table2 below:Table 2. Public availability of specific E. coli strains from which the mutated diderm bacteriumaccording to the invention may be derived by insertion of one or more mutations in the genome. Strain name Genome sequence Available fromBL21(DE3) Genbank CP001509.3 (Jeong HThermofisher scientific et al. 2009. Genome sequences(reference EC0114) of Escherichia coli B strainsNew England Biolabs REL606 and BL21(DE3). J Mol (reference C2527)Biol 394:644–652)HMS174(DE3) (K12-derivative) Mairhofer et al., 2014. Finished Sigma Aldrich / Novagen – ref.Genome Sequence of 69453M Escherichia coli K-12 Strain ATCC 47011 HMS174 (ATCC 47011) GenomeAnnounc. 20142: e00975-14 MG1655 GenBank U00096.3 CGSC, The Coli Genetic StockCenter (Yale University, New Haven) Most preferably, the mutated diderm bacterium is preferably derived from Escherichia coli strain BL21(DE3).In another preferred embodiment, the mutated diderm bacterium belongs to the Pseudomonadalesorder.Preferably, the mutated diderm bacterium belonging to the Pseudomonadales order is derived froma reference bacterium from the same order by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Pseudomonadales order, the mutated diderm bacterium preferably belongs to a familyselected from the group consisting of the Candidatus Azotimanducaceae family, the Ketobacteraceaefamily, the Marinobacteraceae family, the Perlucidibacaceae family, the Pseudohongiellaceae family,the Pseudomonadaceae family, and the Ventosimonadaceae family; more preferably the mutateddiderm bacterium belongs to the Pseudomonadaceae family.Preferably, the mutated diderm bacterium belonging to one of the above families is derived from a reference bacterium from the same family by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations.Within the Pseudomonadaceae family, the mutated diderm bacterium even more preferably is aPseudomonadaceae bacterium of a genera selected from the group consisting of Atopomonas,Azomonas, Azorhizophilus, Azotobacter, Denitrificimonas, Entomomonas, Halopseudomonas,Mesophilobacter, Permianibacter, Pseudomonas, Stutzerimonas, and Thiopseudomonas; even morepreferably the diderm bacterium belongs to the Pseudomonas genus. Preferably, the mutated diderm bacterium belonging to one of the above genera is derived from a reference bacterium from the same genus by insertion in its genome of one or more mutations, preferably by insertion in its genome of one or more non-silent mutations. Preferably, the mutated diderm bacterium belonging to Pseudomonas species is derived from areference bacterium from Pseudomonasspecies by insertion in its genome of one or more mutations,preferably by insertion in its genome of one or more non-silent mutations. TARGET(S) OF THE MUTATION(S) In a first aspect, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes). In an embodiment, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in energy production and / or energy conversion. In this case, the gene(s) encoding proteins involved in energy production and / or energy conversion is(are) preferably selected from the group consisting of: ^narG (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_01202), ^nuoC (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02211), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in narG, nuoC, or any combination thereof, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium: -narG (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_01202): a position in the genome of the mutated bacterium equivalent to position1271070 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes (i.e. after optimal global alignment of the genomes of E. coli strain BL21(DE3) andthe genome of the mutated bacterium); -nuoC (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02211): a position in the genome of the mutated bacterium equivalent to position2289710 in the genome of E. coli strain BL21(DE3), after optimal global alignment bothgenomes; or- any combination thereof.In some cases (e.g. when the genome of the mutated bacterium comprises only one mutationcompared to the genome of E. coli strain BL21(DE3), or when the genome of the mutated bacteriumcomprises only substitutions compared to the genome of E. coli strain BL21(DE3)), the positionequivalent to a particular position in the genome of E. coli strain BL21(DE3) is the same position. Inother cases, a skilled person can determine the equivalent position by obtaining an optimal globalalignment of the genomes of E. coli strain BL21(DE3) and the genome of the mutated bacterium. Theequivalent position in the genome of the mutated bacterium is the position in the genome of themutated bacterium that is aligned to the position of interest in the genome of E. coli strain BL21(DE3)in the optimal global alignment. When a mutation is present at one or more of the above positions in genes narG, nuoC, or any combination thereof, the mutation is preferably selected from: ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 1271070 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 3059 in the narG gene at locus ECD_01202), after optimal global alignmentof both genomes, resulting in a substitution, by another amino acid, of the histidine (His orH) amino acid residue at a position in the narG protein of the mutated bacterium equivalent to position 1020 of the narG protein of E. coli strain BL21(DE3) after optimal global alignmentof both protein sequences (i.e. after optimal global alignment of the narG protein sequenceof the mutated bacterium and the narG protein sequence of E. coli strain BL21(DE3)).In some cases (e.g. when the genome of the mutated bacterium comprises only one mutation compared to the genome of E. coli strain BL21(DE3), or when the genome of the mutatedbacterium comprises only substitutions compared to the genome of E. coli strain BL21(DE3)),the position equivalent to a particular position in the narG protein of E. coli strain BL21(DE3)is the same position. In other cases, a skilled person can determine the equivalent position by performing an optimal global alignment of the amino acid sequences of the narG protein of E. coli strain BL21(DE3) and the narG protein of the mutated bacterium. The equivalentposition in the narG protein of the mutated bacterium is the position in the genome of the mutated bacterium that is aligned to the position of interest in the narG protein of E. coli strain BL21(DE3) in an optimal global alignment. The other amino acid may be any amino acid other than histidine but may preferably be selected from other positively charged amino acids arginine (Arg or R) and lysine (Lys or K), more preferably histidine is substituted by arginine (Arg or R). In this case, the mutated diderm bacterium preferably expresses a narG protein comprising a H1020R substitution compared to the amino acid sequence of the narG protein of E. coli strainBL21(DE3)) (Genbank accession number ACT43094.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 2289710 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 1400 in the nuoC gene at locus ECD_02211), after optimal global alignmentof both genomes, resulting in a substitution, by another amino acid, of the valine (Val or V)amino acid residue at a position in the nuoC protein of the mutated bacterium equivalent toposition 467 in the nuoC protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than valine but may preferably be selected from other hydrophobic amino acids (alanine (Ala or A), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M), phenylalnine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from other hydrophobic aliphatic amino acids (alanine (Ala or A), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably valine is substituted by alanine (Ala or A). In this case, the mutated diderm bacterium preferably expresses a nuoC protein comprising aV467A substitution compared to the amino acid sequence of the nuoC protein of E. colistrain BL21(DE3)) (Genbank accession number ACT44033.1); and ^Any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in cell cycle control, cell division, chromosome partitioning, and any combination thereof. In this case, the gene(s) encoding proteins involved in cell cycle control, cell division, chromosome partitioning, and any combination thereof is preferably etk (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00984). When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, a mutation in etk, then the mutation is preferably located at a position in the genome ofthe mutated bacterium equivalent to position 1047795 in the genome of E. coli strain BL21(DE3)(corresponding to relative position 1505 in the etk gene at locus ECD_00984), after optimal globalalignment of both genomes. More preferably, the mutation is a single nucleotide polymorphism (SNP) at a position in the genomeof the mutated bacterium equivalent to position 1047795 in the genome of E. coli strain BL21(DE3)(corresponding to relative position 1505 in the etk gene at locus ECD_00984), after optimal globalalignment of both genomes, resulting in a substitution, by another amino acid, of the leucine (Leu orL) amino acid residue at a position in the etk protein of the mutated bacterium equivalent to position502 in the etk protein of E. coli strain BL21(DE3), after optimal global alignment of both proteinsequences. The other amino acid may be any amino acid other than leucine but may preferably be selected fromnon-polar amino acids; preferably from alanine, valine, isoleucine, and proline; more preferablyleucine is substituted by proline (Pro or P). In this case, the mutated diderm bacterium preferably expresses an etk protein comprising a L502Psubstitution compared to the amino acid sequence of the etk protein of E. coli strain BL21(DE3))(Genbank accession number ACT42879.1). Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in nucleotide transport and / or nucleotide metabolism. In this case, the gene(s) encoding proteins involved in nucleotide transport and / or nucleotide metabolism is preferably selected from the group consisting of: ^speD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00119) ^pgi (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03897), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which itis derived, one or more mutation(s) in speD, pgi or any combination thereof, then the mutation(s)is(are) preferably located at the following positions in the genome of the mutated bacterium: -speD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00119) : a position in the genome of the mutated bacterium equivalent to position137789 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 598 inthe speD gene at locus ECD_00119), after optimal global alignment of both genomes;- pgi (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03897): a position in the genome of the mutated bacterium equivalent to position4142045 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 917 inthe pgi gene at locus ECD_03897), after optimal global alignment of both genomes; or- any combination thereof.When a mutation is present at one or more of the above positions in genes speD and pgi, the mutation is preferably selected from: ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 137789 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 598 in the speD gene at locus ECD_00119), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the tyrosine (Tyr or Y)amino acid residue at a position in the speD protein of the mutated bacterium equivalent to position 200 of the speD protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than tyrosine but may preferably be selected from positively charged amino acids histidine (His or H), arginine (Arg or R) and lysine (Lys or K), more preferably tyrosine is substituted by histidine (His or H). In this case, the mutated diderm bacterium preferably expresses a speD protein comprising a Y200H substitution compared to the amino acid sequence of the speD protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42020.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 4142045 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 917 in the pgi gene at locus ECD_03897), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the threonine (Thr or T)amino acid residue at a position in the pgi protein of the mutated bacterium equivalent toposition 306 of the pgi protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than threonine but may preferably be selected from hydrophobic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M), phenylalnine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from hydrophobic aliphatic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably threonine is substituted by isoleucine (Ile or I). In this case, the mutated diderm bacterium preferably expresses a pgi protein comprising aT306I substitution compared to the amino acid sequence of the pgi protein of E. coli strainBL21(DE3)) (Genbank accession number ACT45688.1); and ^any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus,species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteinsinvolved in carbohydrate transport and / or carbohydrate metabolism. In this case, the gene(s) encoding proteins involved in carbohydrate transport and / or carbohydrate metabolism is preferably selected from the group consisting of: ^ygbM (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02589), ^garK (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02989), ^ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_00874), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which itis derived, one or more mutation(s) in ygbM, garK, ybjT or any combination thereof, the mutation(s)is(are) preferably located at the following positions in the genome of the mutated bacterium: -ygbM (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02589): a position in the genome of the mutated bacterium equivalent to position2704598 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 395 inthe ygbM gene at locus ECD_02589), after optimal global alignment of both genomes;- garK (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02989: a position in the genome of the mutated bacterium equivalent to position3137823 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 142 ingarK gene at locus ECD_02989), after optimal global alignment of both genomes;- ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_00874) : a position in the genome of the mutated bacterium equivalent to position912803 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 184 inthe ybjT gene at locus ECD_00874), after optimal global alignment of both genomes; or- any combination thereof.When a mutation is present at one or more of the above positions in genes ygbM, garK and ybjT, the mutation is preferably selected from: ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 2704598 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 395 in the ygbM gene at locus ECD_02589), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the arginine (Arg or R)amino acid residue at a position in the ygbM protein of the mutated bacterium equivalent toposition 132 of the ygbM of E. coli strain BL21(DE3) after optimal global alignment of bothprotein sequences.The other amino acid may be any amino acid other than arginine but may preferably be selected from other positively charged amino acids histidine (His or H) and lysine (Lys or K), more preferably arginine is substituted by histidine (His or H). In this case, the mutated diderm bacterium preferably expresses a ygbM protein comprising aR132H substitution compared to the amino acid sequence of the ygbM protein of E. colistrain BL21(DE3)) (Genbank accession number ACT44408.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 3137823 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 142 in garK gene at locus ECD_02989), after optimal global alignment of bothgenomes, resulting in a substitution, by another amino acid, of the threonine (Thr or T) aminoacid residue at a position in the garK protein of the mutated bacterium equivalent to position48 of the garK protein E. coli strain BL21(DE3) after optimal global alignment of both proteinsequences. The other amino acid may be any amino acid other than threonine but may preferably be selected from hydrophobic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M), phenylalnine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from hydrophobic aliphatic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably threonine is substituted by alanine (Ala or A). In this case, the mutated diderm bacterium preferably expresses a garK protein comprising a T48A substitution compared to the amino acid sequence of the garK protein of E. coli strainBL21(DE3)) (Genbank accession number ACT44793.2). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 912803 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 184 in the ybjT gene at locus ECD_00874), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the alanine (Ala or A) amino acid residue at a position in the ybjT protein of the mutated bacterium equivalent toposition 62 of the ybjT protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences. The other amino acid may be any amino acid other than alanine but may preferably be selected from leucine, isoleucine, valine, and proline; more preferably alanine is substituted by proline (Pro or P). In this case, the mutated diderm bacterium preferably expresses a ybjT protein comprising a A62P substitution compared to the amino acid sequence of the ybjT protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42769.1); and ^any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in lipid transport and / or lipid metabolism. In this case, the gene(s) encoding proteins involved in lipid transport and / or lipid metabolism is preferably cdsA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00173). When the mutated diderm bacterium comprises, compared to the reference bacterium from which itis derived, a mutation in cdsA, the mutation is preferably located at a position in the genome of themutated bacterium equivalent to position 199016 in the genome of E. coli strain BL21(DE3)(corresponding to relative position 497 in the cdsA gene at locus ECD_00173), after optimal globalalignment of both genomes. More preferably, the mutation is preferably a single nucleotide polymorphism (SNP) at a position inthe genome of the mutated bacterium equivalent to position 199016 in the genome of E. coli strainBL21(DE3) (corresponding to relative position 497 in the cdsA gene at locus ECD_00173), after optimalglobal alignment of both genomes, resulting in a substitution, by another amino acid, of the serine(Ser or S) amino acid residue at a position in the cdsA protein of the mutated bacterium equivalentto position 166 of the cdsA protein of E. coli strain BL21(DE3)) after optimal global alignment of bothprotein sequences.The other amino acid may be any amino acid other than serine but may preferably be selected from hydrophobic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M), phenylalanine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from hydrophobic aromatic amino acids (phenylalanine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), more preferably serine is substituted by phenylalanine (Phe or F).In this case, the mutated diderm bacterium preferably expresses a cdsA protein comprising a S166Fsubstitution compared to the amino acid sequence of the cdsA protein of E. coli strain BL21(DE3))(Genbank accession number ACT42074.1). Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in translation, ribosomal structure ribosomal biogenesis, and any combination thereof. In this case, the gene(s) encoding proteins involved in translation, ribosomal structure ribosomal biogenesis, and any combination thereof is preferably selected from: ^ligT (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00146), ^rpsA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00915), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in ligT, rpsA, or any combination thereof, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium: -ligT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag: ECD_00146) : a position in the genome of the mutated bacterium equivalent to position164564 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 320 inthe ligT gene at locus ECD_00146), after optimal global alignment of both genomes;- rpsA (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag: ECD_00915): a position in the genome of the mutated bacterium equivalent to position968210 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 1126 inthe rpsA gene at locus ECD_00915), after optimal global alignment of both genomes); or- any combination thereof.When a mutation is present at one or more of the above positions in genes ligT and rpsA, the mutationis preferably selected from:^ a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 164564 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 320 in the ligT gene at locus ECD_00146), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the arginine (Arg or R)amino acid residue at a position in the ligT protein of the mutated bacterium equivalent toposition 107 of the ligT protein of E. coli strain BL21(DE3)) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than arginine but may preferably be selected from other positively charged amino acids histidine (His or H) and lysine (Lys or K), more preferably arginine is substituted by histidine (His or H). In this case, the mutated diderm bacterium preferably expresses a ligT protein comprising a R107H substitution compared to the amino acid sequence of the ligT protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42047.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 968210 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 1126 in the rpsA gene at locus ECD_00915), after optimal global alignmentof both genomes, resulting in a substitution, by another amino acid, of the aspartic acid (Aspor D) amino acid residue at a position in the rpsA protein of the mutated bacterium equivalentto position 376 of the rpsA protein of E. coli strain BL21(DE3)) after optimal global alignmentof both protein sequences.The other amino acid may be any amino acid other than aspartic acid but may preferably be selected from polar uncharged amino acids (serine (Ser or S), threonine (Thr or T), Asparagine (Asn) and glutamine (Gln or Q)), more preferably aspartic acid is substituted by asparagine (Asn or N). In this case, the mutated diderm bacterium preferably expresses a rpsA protein comprising a D376N substitution compared to the amino acid sequence of the rpsA protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42810.1); and ^any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in transcription. In this case, the gene(s) encoding proteins involved in transcription is preferably selected from the group consisting of: ^ydcl (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_01379), ^yfeR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02308), ^ompR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3,locus tag: ECD_03257), ^basR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03984), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in ydcl, yfeR, ompR, basR, or any combination thereof, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium: -ydcl (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_01379): a position in the genome of the mutated bacterium equivalent to position1449046 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 88 inthe ydcl gene at locus ECD_01379), after optimal global alignment of both genomes;- yfeR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_02308): a position in the genome of the mutated bacterium equivalent to position2399087 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 157 inthe yfeR gene at locus ECD_02308), after optimal global alignment of both genomes;- ompR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3,locus tag: ECD_03257: a position in the genome of the mutated bacterium equivalent toposition 3396345 in the genome of E. coli strain BL21(DE3) (corresponding to relative position620 in the ompR gene at locus ECD_03257), after optimal global alignment of both genomes;- basR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03984): a position in the genome of the mutated bacterium equivalent to position4240680 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 350 inthe basR gene at locus ECD_03984), after optimal global alignment of both genomes; or- any combination thereof.When a mutation is present at one or more of the above positions in genes ydcl, yfeR, ompR, basR,and any combination thereof, the mutation is preferably selected from:^ a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 1449046 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 88 in the ydcl gene at locus ECD_01379), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the arginine (Arg or R)amino acid residue at a position in the ydcl protein of the mutated bacterium equivalent toposition 30 of the ydcl protein of E. coli strain BL21(DE3)) after optimal global alignment ofboth protein sequences. The other amino acid may be any amino acid other than arginine but may preferably be selected from positively charged polar amino acids; preferably from histidine, lysine, andcysteine; more preferably arginine is substituted by cysteine (Cys or C).In this case, the mutated diderm bacterium preferably expresses a ydcl protein comprising a R30C substitution compared to the amino acid sequence of the ydcl protein of E. coli strainBL21(DE3)) (Genbank accession number ACT43263.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 2399087 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 157 in the yfeR gene at locus ECD_02308), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the threonine (Thr or T)amino acid residue at a position in the yfeR protein of the mutated bacterium equivalent toposition 53 of the encoded yfeR protein (or a position equivalent to position 53 in the amino acid sequence of encoded protein yfeR after optimal global alignment with the amino acid sequence of the protein yfeR of E. coli strain BL21(DE3)) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than threonine but may preferably be selected from hydrophobic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M), phenylalanine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from hydrophobic aliphatic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably threonine is substituted by alanine (Ala or A). In this case, the mutated diderm bacterium preferably expresses a yfeR protein comprising a T53A substitution compared to the amino acid sequence of the yfeR protein of E. coli strainBL21(DE3)) (Genbank accession number ACT44129.1).^ a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 3396345 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 620 in the ompR gene at locus ECD_03257), after optimal global alignmentof both genomes, resulting in a substitution, by another amino acid, of the arginine (Arg or R) amino acid residue at a position in the ompR protein of the mutated bacterium equivalentto position 207 of the ompR protein of E. coli strain BL21(DE3) after optimal global alignmentof both protein sequences. The other amino acid may be any amino acid other than arginine but may preferably be selected from other positively charged amino acids lysine (Lys or K) and histidine (His or H), more preferably arginine is substituted by histidine (His or H). In this case, the mutated diderm bacterium preferably expresses a ompR protein comprising aR207H substitution compared to the amino acid sequence of the ompR protein of E. colistrain BL21(DE3)) (Genbank accession number ACT45060.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 4240680 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 350 in the basR gene at locus ECD_03984), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of arginine (Arg or R) amino acid residue at a position in the basR protein of the mutated bacterium equivalent to position117 of the basR protein of E. coli strain BL21(DE3) after optimal global alignment of bothprotein sequences. The other amino acid may be any amino acid other than arginine but may preferably be selected from polar uncharged amino acids (serine (Ser or S), threonine (Thr or T), Asparagine (Asn) and glutamine (Gln or Q)), more preferably arginine is substituted by Glutamine (Gln or Q). In this case, the mutated diderm bacterium preferably expresses a basR protein comprising a R117Q substitution compared to the amino acid sequence of the basR protein of E. coli strainBL21(DE3)) (Genbank accession number ACT45774.1); and ^any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in cell wall biogenesis, cell membrane biogenesis, cell envelope biogenesis, and any combination thereof. In this case, the gene(s) encoding proteins involved in cell wall biogenesis, cell membrane biogenesis, cell envelope biogenesis, and any combination thereof is preferably selected from the group consisting of: ^ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3,locus tag : ECD_00874), ^etk (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00984), and^ any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in ybjT, etk, or any combination thereof, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium: -ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_00874) : a position in the genome of the mutated bacterium equivalent to position912803 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 184 inthe ybjT gene at locus ECD_00874), after optimal global alignment of both genomes;- etk (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00984): a position in the genome of the mutated bacterium equivalent to position1047795 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 1505 inthe etk gene at locus ECD_00984), after optimal global alignment of both genomes; or- any combination thereof.When a mutation is present at one or more of the above positions in genes ybjT and / or etk, themutation is preferably selected from:^ a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 912803 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 184 in the ybjT gene at locus ECD_00874), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the alanine (Ala or A)amino acid residue at a position in the ybjT protein of the mutated bacterium equivalent toposition 62 of the ybjT protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences.The other amino acid may be any amino acid other than alanine but may preferably be selected from leucine, isoleucine, valine, and proline; more preferably alanine is substitutedby proline (Pro or P). In this case, the mutated diderm bacterium preferably expresses a ybjT protein comprising a A62P substitution compared to the amino acid sequence of the ybjT protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42769.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 1047795 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 1505 in the etk gene at locus ECD_00984), after optimal global alignment ofboth genomes, resulting in a substitution, by another amino acid, of the leucine (Leu or L) amino acid residue at a position in the etk protein of the mutated bacterium equivalent to position 502 in the etk protein of E. coli strain BL21(DE3), after optimal global alignment ofboth protein sequences. The other amino acid may be any amino acid other than leucine but may preferably be selected from non-polar amino acids; preferably from alanine, valine, isoleucine, and proline;more preferably leucine is substituted by proline (Pro or P). In this case, the mutated diderm bacterium preferably expresses an etk protein comprising a L502P substitution compared to the amino acid sequence of the etk protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42879.1); and^ any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in intracellular trafficking, secretion, vesicular transport, and any combination thereof. In this case, the gene(s) encoding proteins involved in intracellular trafficking, secretion, vesicular transport, and any combination thereof is preferably tcyP (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_01698, also referred to as gene “ydjN”). When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, a mutation in tcyP gene, the mutation is preferably located at a position in the genome ofthe mutated bacterium equivalent to position 1755734 in the genome of E. coli strain BL21(DE3)(corresponding to relative position 388 in the tcyP gene at locus ECD_01698), after optimal globalalignment of both genomes. More preferably, the mutation is a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacterium equivalent to position 1755734 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 388 in the tcyP gene at locus ECD_01698), after optimal globalalignment of both genomes, resulting in a substitution, by another amino acid, of the phenylalanine(Phe or F) amino acid residue at a position in the tcyP protein of the mutated bacterium equivalentto position 130 of the tcyP protein of E. coli strain BL21(DE3) after optimal global alignment of bothprotein sequences.The other amino acid may be any amino acid other than phenylalanine but may preferably be selected from other hydrophobic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), methionine (Met or M), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably from hydrophobic aliphatic amino acids (alanine (Ala or A), valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably phenylalanine is substituted by Leucine (Leu or L). In this case, the mutated diderm bacterium preferably expresses a tcyP protein comprising a F130Lsubstitution compared to the amino acid sequence of the tcyP protein of E. coli strain BL21(DE3))(Genbank accession number ACT43553.1). Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in signal transduction mechanisms. In this case, the gene(s) encoding proteins involved in signal transduction mechanisms is preferably pyrS (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_02290, also referred to as “ypdA”). When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in pyrS, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium:pyrS (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02290, also referred to as “ypdA”): aposition in the genome of the mutated bacterium equivalent to position 2376813 in the genome of E.coli strain BL21(DE3) (corresponding to relative position 257 in the pyrS gene at locus ECD_02290),after optimal global alignment of both genomes. When a mutation is present at one or more of the above positions in genes pyrS, the mutation ispreferably a single nucleotide polymorphism (SNP) at a position in the genome of the mutatedbacterium equivalent to position 2376813 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 257 in the pyrS gene at locus ECD_02290), after optimal global alignment of bothgenomes, resulting in a substitution, by another amino acid, of the glycine (Gly or G) amino acidresidue at a position in the pyrS protein of the mutated bacterium equivalent to position 86 of thepyrS protein of E. coli strain BL21(DE3) after optimal global alignment of both protein sequences.The other amino acid may be any amino acid other than glycine but may preferably be selected from negatively charged amino acids aspartic acid (Asp or D) and glutamic acid (Glu or E), more preferably glycine is substituted by aspartic acid (Asp or D). In this case, the mutated diderm bacterium preferably expresses a pyrS protein comprising a G86Dsubstitution compared to the amino acid sequence of the pyrS protein of E. coli strain BL21(DE3))(Genbank accession number ACT44111.1). Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in a gene (i.e. one or more genes) encoding proteins involved in inorganic ion transport and / or inorganic ion metabolism. In this case, the gene encoding proteins involved in inorganic ion transport and / or inorganic ionmetabolism is preferably selected from the group consisting of:^ cydD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00891), ^dcuD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3,locus tag: ECD_03087), and ^any combination thereof.When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in cydD, dcuD, or any combination thereof, the mutation(s) is(are) preferably located at the following positions in the genome of the mutated bacterium: -cydD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00891): a position in the genome of the mutated bacterium equivalent to position934275 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 1744 inthe cydD gene at locus ECD_00891), after optimal global alignment of both genomes;- dcuD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03087): a position in the genome of the mutated bacterium equivalent to position3236544 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; or -any combination thereof.When a mutation is present at one or more of the above positions in genes cydD and / or dcuD, themutation is preferably selected from: ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 934275 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 1744 in the cydD gene at locus ECD_00891), after optimal global alignmentof both genomes, resulting in a substitution, by another amino acid, of the alanine (Ala or A) amino acid residue at a position in the cydD protein of the mutated bacterium equivalent toposition 582 of the cydD protein of E. coli strain BL21(DE3) after optimal global alignment ofboth protein sequences. The other amino acid may be any amino acid other than alanine but may preferably be selected from polar uncharged amino acids (serine (Ser or S), threonine (Thr or T), Asparagine (Asn) and glutamine (Gln or Q)), more preferably alanine is substituted by threonine (Thr or T). In this case, the mutated diderm bacterium preferably expresses a cydD protein comprising a A582T substitution compared to the amino acid sequence of the cydD protein of E. coli strainBL21(DE3)) (Genbank accession number ACT42786.1). ^a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacteriumequivalent to position 3236544 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 513 in the dcuD gene at locus ECD_03087), after optimal global alignment of both genomes, resulting in a stop codon at a position in the dcuD protein of the mutated bacterium equivalent to position 171 in the dcuD protein of E. coli strain BL21(DE3) afteroptimal global alignment of both protein sequences. In this case, the mutated diderm bacterium preferably expresses a dcuD protein corresponding to the dcuD protein of E. coli strain BL21(DE3) (Genbank accession numberACT44891.1) truncated at position 170; and ^any combination thereof.Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus,species or strain disclosed above) is mutated in the gene yjgL (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_04119). When the mutated diderm bacterium comprises, compared to the reference bacterium from which itis derived, one or more mutation(s) in gene yjgL (GenBank identification number for Escherichia colistrain BL21(DE3): CP001509.3, locus tag : ECD_04119), the mutation(s) is(are) preferably located at a position in the genome of the mutated bacterium equivalent to position 4387431 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 353 in the yjgL gene at locus ECD_04119), after optimal global alignment of both genomes. More preferably, when a mutation is present at one or more of the above positions in gene yjgL, the mutation is a single nucleotide polymorphism (SNP) at a position in the genome of the mutated bacterium equivalent to position 4387431 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 353 in the yjgL gene at locus ECD_04119), after optimal global alignment of bothgenomes, resulting in a substitution, by another amino acid, of the glutamic acid (Glu or E) aminoacid residue at a position in the yjgL protein of the mutated bacterium equivalent to position 118 ofthe yjgL protein of E. coli strain BL21(DE3) after optimal global alignment of both protein sequences.The other amino acid may be any amino acid other than glutamic acid but may preferably be selectedfrom glycine and alanine; more preferably glutamic acid is substituted by glycine (Gly or G).In this case, the mutated diderm bacterium preferably expresses a yjgL protein comprising a E118Gsubstitution compared to the amino acid sequence of the yjgL protein of E. coli strain BL21(DE3))(Genbank accession number ACT45907.1). Alternatively or in combination, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in the gene yqjA (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_02964). When the mutated diderm bacterium comprises, compared to the reference bacterium from which it is derived, one or more mutation(s) in gene yqjA, the mutation(s) is(are) preferably located at aposition in the genome of the mutated bacterium equivalent to position 3114100 in the genome of E.coli strain BL21(DE3) (corresponding to relative position 29 in the yqjA gene at locus ECD_02964),after optimal global alignment of both genomes.More preferably, when a mutation is present at one or more of the above positions in gene ygjA, themutation is a single nucleotide polymorphism (SNP) at a position in the genome of the mutatedbacterium equivalent to position 3114100 in the genome of E. coli strain BL21(DE3) (corresponding torelative position 29 in the yqjA gene at locus ECD_02964), after optimal global alignment of bothgenomes, resulting in a substitution, by another amino acid, of the alanine (Ala or A) amino acidresidue at a position in the yqjA protein of the mutated bacterium equivalent to position 10 of theyqjA protein of E. coli strain BL21(DE3) after optimal global alignment of both protein sequences.The other amino acid may be any amino acid other than alanine but may preferably be selected from other hydrophobic amino acids (valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine(Met or M), phenylalanine (Phe or F), tyrosine (Tyr or Y) and tryptophan (Trp or W)), preferably fromother hydrophobic aliphatic amino acids (valine (Val or V), isoleucine (Iso or I), leucine (Leu or L), methionine (Met or M)), more preferably alanine is substituted by valine (Val or V). In this case, the mutated diderm bacterium preferably expresses a yqjA protein comprising a A10Vsubstitution compared to the amino acid sequence of the yqjA protein of E. coli strain BL21(DE3))(Genbank accession number ACT44768.1). In a second aspect, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) is mutated in an intergenic region. In this case, the intergenic region is preferably selected from regions involved in the regulation of gene expression, more preferably from the group consisting of:(i) the intergenic region located between gene paoA (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00245) and gene yagU (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00246), (ii) the intergenic regions located between gene yfgO (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02385) and gene bepA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02386), (iii) the intergenic regions located between gene rluD (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02484) and gene bamD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02485), and (iv) any combination thereof.In this case, the mutation(s) in the above intergenic regions is(are) preferably located at: (i) a position in the genome of the mutated bacterium equivalent to position 272841 in thegenome of E. coli strain BL21(DE3) (in the intergenic region located between gene paoA(GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00245) and gene yagU (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00246)), after optimal global alignment of bothgenomes, (ii) a position in the genome of the mutated bacterium equivalent to position 2480418 in thegenome of E. coli strain BL21(DE3) (in the intergenic regions located between gene yfgO(GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02385) and gene bepA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02386)), after optimal global alignment of bothgenomes, (iii) a position in the genome of the mutated bacterium equivalent to position 2602632 in thegenome of E. coli strain BL21(DE3) (in the intergenic regions located between gene rluD(GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02484) and gene bamD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02485)), after optimal global alignment of bothgenomes, or (iv) any combination thereof.In any of the above positions, the mutation is preferably a single nucleotide polymorphism (SNP). More preferably, the mutation(s) in the above intergenic regions is(are) preferably: (i) a substitution of a cytosine (C) by a thymidine (T) at a position in the genome of the mutatedbacterium equivalent to position 272841 in the genome of E. coli strain BL21(DE3) (inintergenic regions surrounding the gene paoA at locus ECD_00245), after optimal globalalignment of both genomes,(ii) a substitution of a guanine (G) by a adenine (A) at a position in the genome of the mutatedbacterium equivalent to position 2480418 in the genome of E. coli strain BL21(DE3) (inintergenic regions surrounding the gene yfgO at locus ECD_02385), after optimal globalalignment of both genomes, (iii) a substitution of a thymidine (T) by a cytosine (C) at a position in the genome of the mutatedbacterium equivalent to position 2602632 in the genome of E. coli strain BL21(DE3) (inintergenic regions surrounding the gene rluD at locus ECD_02484), after optimal globalalignment of both genomes, or (iv) any combination thereof.Table 3 below summarizes the preferred genes and intergenic regions and the preferred positions inwhich the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) may comprise mutations, as well as the preferred mutations. Table 3. Preferred genes and intergenic regions in which the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) may comprise mutations. The indicatedposition is the position in the genome of E. coli strain BL21(DE3) (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3), to which the mutated position in the mutated diderm bacterium of the invention is equivalent. The indicated relative position is the position in the gene ofinterest of E. coli strain BL21(DE3) to which the mutated position in the mutated diderm bacteriumof the invention is equivalent: Gene / Gene Mutation Position in Locus tag in Relative Protein intergenic eggNOG v5 (wt / CP001509.3 CP001509.3 position mutation region category mutated) 11271070 ECD_01202 3059 narG C A / G H1020R2 2289710 ECD_02211 1400 nuoC C A / G V467A3 3236544 ECD_03087 513 dcuD P G / A W171Stop4 1047795 ECD_00984 1505 etk D, M A / G L502P5 137789 ECD_00119 598 speD F A / G Y200H6 2704598 ECD_02589 395 ygbM G G / A R132H7 3137823 ECD_02989 142 garK G T / C T48A8 4142045 ECD_03897 917 pgi F C / T T306I9 199016 ECD_00173 497 cdsA I C / T S166F10 164564 ECD_00146 320 ligT J C / T R107H11 968210 ECD_00915 1126 rpsA J G / A D376N12 1449046 ECD_01379 88 ydcI K G / A R30C13 2399087 ECD_02308 157 yfeR K T / C T53A14 912803 ECD_00874 184 ybjT G, M C / G A62P15 1755734 ECD_01698 388 tcyP U T / C F130L16 3114100 ECD_02964 29 yqjA S C / T A10V17 2376813 ECD_02290 257 pyrS T G / A G86D18 3396345 ECD_03257 620 ompR K C / T R207H19 4240680 ECD_03984 350 basR K C / T R117Q20 934275 ECD_00891 1744 cydD P C / T A582T21 4387431 ECD_04119 353 yjgL S A / G E118G22 Between Between ECD_00245 272841 / paoA andF, S C / T / and yagU ECD_00246 23 Between Between ECD_02385 2480418 / yfgO andS, S G / A / and bepA ECD_02386 24 Between Between ECD_02484 2602632 / rluD andJ, M T / C / and bamD ECD_02485 The mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) may comprise mutations in 2 or more (including 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, 9 or more, 10 or more, 11 or more, 12 or more, 13 or more, 14 or more, 15 or more, 16 or more, 17 or more, 18 or more, 19 or more, 20 or more, 21 or more, 22 or more, 23 or more or even all 24) of the genes and intergenic regions disclosed above. Each mutation is preferably located at the positions defined above. More preferably, the mutations are selected from the SNPs disclosed above. In particular, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) may comprise mutations in 2 or more (including 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, 9 or more, 10 or more, 11 or more, 12 or more, 13 or more, 14 or more, 15 or more, 16 or more, 17 or more, 18 or more, 19 or more, 20 or more, or even all 21) of the genes disclosed above. Each mutation is preferably located at the positions defined above. More preferably, the mutations are selected from the SNPs disclosed above. Alternatively, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) may comprise mutations in 2 or more (including all) of the intergenic regions disclosed above (in particular at the defined positions and with the defined SNPs). In an embodiment, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) comprises a mutation in each of the 24 above disclosed genes and intergenic regions. Preferably, the mutations are located at the positions defined above. More preferably, the mutations are the SNPs disclosed above. In a preferred embodiment, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) comprise one mutation or more in one gene or more encoding proteins involved in cell wall biogenesis, cell membrane biogenesis, cell envelope biogenesis, and any combination thereof (eggNOG v5 category M), more preferably in the genes defined above as belonging to this category. Each mutation is preferably located at the positions defined above. More preferably, the mutations are selected from the SNPs disclosed above. TYPE OF MUTATIONS The mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention comprises one or more mutations in their genome compared to the genome of the reference diderm bacterium from which they derive. Its tolerance to elevated concentrations of amine compounds is the consequence of the one or more of the mutations inserted into its genome compared to the genome of the reference diderm bacterium from which it derives. As a result, one or more of the mutations inserted into their genome compared to the genome of the reference diderm bacterium from which they derive is a non-silent mutation, which confers tolerance to higher concentrations of amine compounds than the reference bacterium from which they derive. When the mutated diderm bacterium according to the invention comprises only one mutation into its genome compared to the genome of the reference diderm bacterium from which it derives, this mutation is non-silent. When the mutated diderm bacterium according to the invention comprises several mutations into its genome compared to the genome of the reference diderm bacterium from which it derives, one or more (such as 2, 3, 4, 5… or all) of the mutations is(are) non-silent. Non-silent mutations are preferably selected from: ^Mutations in the open-reading frame that alter the amino acid sequence of the encodedprotein, in particular selected from: osubstitution of one or more nucleotides in the open-reading frame resulting in:^ a change of one or more amino acids of the encoded protein, or^ the insertion of a stop codon, leading to a truncated encoded protein,o deletion of one or more nucleotides in the open-reading frame resulting in:^ deletion of one or more amino acids of the encoded protein (if the numberof deleted nucleotides is a multiple of three), or ^a reading frame shift (if the number of deleted nucleotides is not a multipleof three, the sequence of the protein is then more importantly changed), ando insertion of one or more nucleotides in the open-reading frame resulting in:^ insertion of one or more amino acids in the encoded protein (if the numberof deleted nucleotides is a multiple of three), or ^a reading frame shift (if the number of deleted nucleotides is not a multipleof three, the sequence of the protein is then more importantly changed), and ^Mutations in a regulatory sequence (promoter, enhancer, splicing site…) of a gene that alter:o the expression level of the encoded protein (mutation in promoter, enhancer…), oro the sequence of the encoded protein(s) (mutation in splicing site).Preferred non-silent mutations include: ^substitutions of 1 to 3 (i.e. 1, 2 or 3, preferably 1, i.e. a single nucleotide polymorphism or“SNP”) nucleotide(s) in an open-reading frame resulting in the substitution of one amino acid by a distinct amino acid in the encoded protein, ^substitutions of 1 to 3 (i.e. 1, 2 or 3, preferably 1, i.e. an SNP) nucleotide(s) in an open-reading frame resulting in a stop codon leading to a truncated encoded protein, ^short insertions of 1 or 2 (preferably 1, i.e. an SNP) nucleotide(s) in an open-reading frameresulting in a reading frame shift, and ^short deletions of 1 or 2 (preferably 1, i.e. an SNP) nucleotide(s) in an open-reading frameresulting in a reading frame shift. Preferably, the mutation is a substitution and more preferably results in an amino acid substitution in the amino acid sequence of the protein encoded by the gene comprising the mutation, preferably wherein the mutation enhances the function of the protein encoded by the gene comprising the mutation. TOLERANCE TO ELEVATED CONCENTRATIONS OF AMINE COMPOUNDS The mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to elevated concentrations of one or more amine compound(s), i.e. the MIC(s) of the one or more amine compound(s) required to prevent growth of the mutated bacterium is higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) thanthe corresponding MIC(s) for the reference bacterium from which it is derived (such as Escherichiacoli strain BL21(DE3)). In this case, no matter from which reference bacterium the mutated bacterium is derived, the MIC(s) of one or more amine compound(s) required to prevent growth of the mutated bacterium is preferably higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MIC(s) for Escherichia coli strain BL21(DE3). Preferably, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosedabove) according to the invention is tolerant to concentrations of one or more amine compound(s) inthe cultivation medium of 15 mM or more, preferably of 20 mM or more, 25 mM or more, 30 mM or more, 35 mM or more, 40 mM or more, 45 mM or more, more preferably of 50 mM or more, 60 mM or more, 70 mM or more, 80 mM or more, 90 mM or more, even more preferably of 100 mM or more, 150 mM or more, 200 mM or more, 250 mM or more, 300 mM or more, 350 mM or more, 400 mM or more,450 mM or more, 500 mM or more (total concentration of the one or more amine compound(s) in thecultivation medium). In a preferred embodiment, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to concentrations of 2 or more (preferably 3 or more, 4 or more, more preferably 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) distinct amine compounds, i.e. the MICs of 2 or more (preferably 3 or more, 4 or more, more preferably 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) distinct amine compounds required to prevent growth of the mutated bacterium are higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICs for the reference bacterium from which it is derived (such as Escherichia coli strain BL21(DE3)). In this case, no matter from which reference bacterium the mutated bacterium is derived, the MICs of the 2 or more (preferably 3 or more, 4 or more, more preferably 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) distinct amine compounds required to prevent growth of the mutated bacterium are preferably higher (preferably at least 1.2 times higher, preferably at least1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, atleast 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICs for Escherichia coli strain BL21(DE3). Preferably, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to concentrations of 2 or more (preferably 3 or more, 4 or more, more preferably 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or even 10 or more) distinct amine compounds in the cultivation medium of 15 mM or more, preferably of 20 mM or more, 25 mM or more, 30 mM or more, 35 mM or more, 40 mM or more, 45 mM or more, more preferably of 50 mM or more, 60 mM or more, 70 mM or more, 80 mM or more, 90 mM or more, even more preferablyof 100 mM or more, 150 mM or more, 200 mM or more, 250 mM or more, 300 mM or more, 350 mM ormore, 400 mM or more, 450 mM or more, 500 mM or more (total concentration of the 2 or more aminecompounds in the cultivation medium).Amine compound(s) to which the mutated diderm bacterium (any class, order, family, genus, speciesor strain disclosed above) according to the invention is tolerant to elevated concentrations are preferably selected from amine compounds of formula (I): wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, said groups being optionally substituted,with proviso that R1 and R2 are not both H, orb) R1 and R2 form together a saturated or non-saturated ring optionally substituted and / oroptionally fused with another ring,and wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl, said groups beingoptionally substituted.Preferably, the amine compound(s) is(are) selected from the group of amine compounds of formula wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, with proviso that R1 and R2 are notboth H, or b) R1 and R2 form together a saturated or non-saturated ring optionally fused with another ring,and wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl.Preferably, in formula (I), R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl,alkenyl, aryl, heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl,heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, with proviso that R1 and R2 are not both H.Preferably, in formula (I) :- R1 and R2 are independently selected from the group consisting of H, C1-C10 alkyl, C1-C10 heteroalkyl,C2-C10 alkenyl, C6-C12 aryl, C4-C12 heteroaryl, C6-C14 heretoaryl alkyl, C7-C14 arylalkyl, C8-C14 aryl alkenyl, C2-C10alkyloxy alkyl, C7-C14aryloxy alkyl, C5-C14heteroaryloxy alkyl and C2-C10alkanoyl alkyl, said groups being optionally substituted (but preferably not substituted) by one or several substituents selected from OH, NH2, SH, NO2, -CN, halogen, C1-C6alkyl, C1-C6alkoxy, C1-C6hydroxyalkyl, C1-C6halogenoalkyl, C1-C6aminoalkyl, -COX,-C(X)3with X being a halogen, CONH2, -COOH, -C(=O)-R, - NHC(=O)R, -C(=O)NHR, -SC(=O)R, -C(=O)SR, -OC(=O)R, and -C(=O)OR, wherein R is a C1-C6 alkyl, with the proviso that R1 and R2 are not simultaneously H, or- R1 and R2 form together a saturated or unsaturated 4-7-member ring optionally substituted (butpreferably not substituted) and optionally fused to another 4-7-member ring, the one or several optional substituent(s) being selected from OH, NH2, SH, NO2, -CN, halogen, oxo group, C1-C6alkyl, C1-C6 alkoxy, C1-C6 hydroxyalkyl, C1-C6 halogenoalkyl, C1-C6 aminoalkyl, -COX,-C(X)3 with X being a halogen, CONH2, -COOH, -C(=O)-R, -NHC(=O)R, -C(=O)NHR, -SC(=O)R, -C(=O)SR, -OC(=O)R, and - C(=O)OR, wherein R is a C1-C6alkyl.In a preferred embodiment, R1 and R2 are independently selected from the group consisting of : H,C1-C10alkyl, C7-C14arylalkyl, C4-C12heteroaryl, C6-C14heretoaryl alkyl, and saturated 4-7 member ring with optionally C1-C6alkyl substituent. Amine compound(s) to which the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to elevated concentrations are more preferably selected from rac-2-aminohexane, rac-2-aminoheptane, cyclohexylamine, furfurylamine, 1-phenylethan-1-amine, n-hexyamine, 5-methylhexan-2-amine, 4-phenyl-2-butylamine, 3- pentylamine, 2-butylamine, but-3-en-1-amine, 2-aminopropan-1-ol, N,2-dimethylpropan-1-amine, N-ethylcyclohexanamine, and any combination thereof. The structures of the compounds are presentedin Table 4 below:Table 4. Preferred amine compounds of which the mutated bacterium of the invention tolerates elevated concentrations: Amine compoundAmine compound name Chemical structurenumber rac-2-aminohexane 1 (IUPAC name : hexan-2- amine) rac-2-aminoheptane (IUPAC name : heptan-2- amine) Cyclohexylamine (IUPAC name : cyclohexanamine) 1-phenylethan-1-amine (IUPAC name : N-methyl- 1-phenylmethanamine) n-hexyamine(IUPAC name : hexan-1-amine) 5-methylhexan-2-amine (IUPAC name : 5- methylhexan-2-amine) 4-phenyl-2-butylamine (IUPAC name : 4- phenylbutan-2-amine) 3-pentylamine (IUPAC name : pentan-3- amine) 2-butylamine (IUPAC name : butan-2- amine) but-3-en-1-amine (IUPAC name : but-3-en- 1-amine) 2-aminopropan-1-ol (IUPAC name : 2- aminopropan-1-ol) N,2-dimethylpropan-1- amine (IUPAC name : N,2- dimethylpropan-1- amine) N-ethylcyclohexanamine 13 (IUPAC name : N- ethylcyclohexanamine) In one embodiment, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to elevated concentrations of rac-2- aminohexane, i.e. the MIC of rac-2-aminohexane required to prevent growth of the mutated bacterium is higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) thanthe corresponding MIC for the reference bacterium from which it is derived (such as Escherichia colistrain BL21(DE3)). In this case, no matter from which reference bacterium the mutated bacterium is derived, the MIC of rac-2-aminohexane required to prevent growth of the mutated bacterium is preferably higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the MIC for Escherichia coli strain BL21(DE3). Preferably, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to concentrations of rac-2-aminohexane in the cultivation medium of 15 mM or more, preferably of 20 mM or more, 25 mM or more, 30 mM or more, 35 mM or more, 40 mM or more, 45 mM or more, more preferably of 50 mM or more, 60 mM or more, 70 mM or more, 80 mM or more, 90 mM or more, even more preferably of 100 mM or more, 150 mM or more, 200 mM or more, 250 mM or more, 300 mM or more, 350 mM or more, 400 mM or more, 450 mM or more, 500 mM or more.In one embodiment, the mutated diderm bacterium (any class, order, family, genus, species or straindisclosed above) according to the invention is tolerant to elevated concentrations of cyclohexylamine,i.e. the MIC of cyclohexylamine required to prevent growth of the mutated bacterium is higher(preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher,at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher,at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICfor the reference bacterium from which it is derived (such as Escherichia coli strain BL21(DE3)).In this case, no matter from which reference bacterium the mutated bacterium is derived, the MIC ofcyclohexylamine required to prevent growth of the mutated bacterium is preferably higher(preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the MIC for Escherichia coli strain BL21(DE3). Preferably, the mutated diderm bacterium (any class, order, family, genus, species or strain disclosed above) according to the invention is tolerant to concentrations of cyclohexylamine in the cultivation medium of 15 mM or more, preferably of 20 mM or more, 25 mM or more, 30 mM or more, 35 mM or more, 40 mM or more, 45 mM or more, more preferably of 50 mM or more, 60 mM or more, 70 mM or more, 80 mM or more, 90 mM or more, even more preferably of 100 mM or more, 150 mM or more, 200 mM or more, 250 mM or more, 300 mM or more, 350 mM or more, 400 mM or more, 450 mM or more, 500 mM or more.In one embodiment, the mutated diderm bacterium (any class, order, family, genus, species or straindisclosed above) according to the invention is tolerant to elevated concentrations of rac-2- aminohexane (IUPAC name : hexan-2-amine), rac-2-aminoheptane (IUPAC name : heptan-2-amine), cyclohexylamine (IUPAC name : cyclohexanamine), 1-phenylethan-1-amine (IUPAC name : hexan-1- amine), n-hexyamine (IUPAC name : N-methyl-1-phenylmethanamine), 5-methylhexan-2-amine (IUPAC name : 5-methylhexan-2-amine), 4-phenyl-2-butylamine (IUPAC name : 4-phenylbutan-2-amine), 3-pentylamine (IUPAC name : pentan-3-amine), 2-butylamine (IUPAC name : butan-2-amine),but-3-en-1-amine (IUPAC name : but-3-en-1-amine), 2-aminopropan-1-ol (IUPAC name : 2-aminopropan-1-ol), N,2-dimethylpropan-1-amine (IUPAC name : N,2-dimethylpropan-1-amine), N-ethylcyclohexanamine (IUPAC name : N-ethylcyclohexanamine), i.e., the MICs of rac-2-aminohexane,rac-2-aminoheptane, cyclohexylamine, 1-phenylethan-1-amine, n-hexyamine, 5-methylhexan-2-amine, 4-phenyl-2-butylamine, 3-pentylamine, 2-butylamine, but-3-en-1-amine, 2-aminopropan-1-ol,N,2-dimethylpropan-1-amine, N-ethylcyclohexanamine, required to prevent growth of the mutatedbacterium are higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) thanthe corresponding MICs for the reference bacterium from which it is derived (such as Escherichia colistrain BL21(DE3)). In this case, no matter from which reference bacterium the mutated bacterium is derived, the MICs of rac-2-aminohexane, rac-2-aminoheptane, cyclohexylamine, 1-phenylethan-1-amine, n-hexyamine, 5-methylhexan-2-amine, 4-phenyl-2-butylamine, 3-pentylamine, 2-butylamine, but-3-en-1-amine, 2-aminopropan-1-ol, N,2-dimethylpropan-1-amine, N-ethylcyclohexanamine, required to preventgrowth of the mutated bacterium are preferably higher (preferably at least 1.2 times higher, preferably at least 1.3 times higher, at least 1.4 times higher, at least 1.5 times higher, at least 1.6 times higher, at least 1.7 times higher, at least 1.8 times higher, at least 1.9 times higher, more preferably at least 2 times higher, at least 2.5 times higher, at least 3 times higher, at least 4 times higher, or even at least 5 times higher) than the corresponding MICs for Escherichia coli strain BL21(DE3). Preferably: (a) The MIC of rac-2-aminohexane for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is at least 30 mM, preferably at least 40 mM, at least 50 mM, at least 60 mM, at least 70 mM, at least 80 mM, orat least 90 mM, (b) The MIC of rac-2-aminoheptane for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is at least 20 mM,preferably at least 25 mM, at least 30 mM, or at least 35 mM,(c) The MIC of cyclohexylamine for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is at least 50 mM,preferably at least 60 mM, at least 70 mM, at least 80 mM, at least 90 mM, at least 100 mM,at least 110 mM, at least 120 mM, or at least 130 mM, (d) The MIC range of 1-phenylethan-1-amine for the mutated diderm bacterium (any class, order,family, genus, species or strain disclosed above) according to the invention is 20 mM to 40mM, and / or the minimum MIC is at least 20 mM, preferably at least 30 mM, preferably about40 mM; (e) The MIC range of n-hexyamine for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is 40 mM to 80 mM, and / or the minimum MIC is at least 40 mM, preferably at least 60 mM, preferably about 80 mM,(f) The MIC range of 5-methylhexan-2-amine for the mutated diderm bacterium (any class, order,family, genus, species or strain disclosed above) according to the invention is 40 mM to 80mM, and / or the minimum MIC is at least 40 mM, preferably at least 60 mM, preferably about80 mM, (g) The MIC range of 4-phenyl-2-butylamine for the mutated diderm bacterium (any class, order,family, genus, species or strain disclosed above) according to the invention is 10 mM to 20 mM, and / or the minimum MIC is at least 10 mM, preferably at least 15 mM, preferably about20 mM, (h) The MIC range of 3-pentylamine for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is 160 mM to 200 mM, and / or the minimum MIC is at least 160 mM, preferably at least 180 mM, preferably about200 mM,(i) The MIC range of 2-butylamine for the mutated diderm bacterium (any class, order, family,genus, species or strain disclosed above) according to the invention is 160 mM to 200 mM, and / or the minimum MIC is at least 160 mM, preferably at least 180 mM, preferably about 200 mM,, (j) The MIC range of but-3-en-1-amine for the mutated diderm bacterium (any class, order,family, genus, species or strain disclosed above) according to the invention is 200 mM to 250 mM, and / or the minimum MIC is at least 200 mM, preferably at least 220 mM, preferably about 250 mM,, (k) The MIC range of 2-aminopropan-1-ol for the mutated diderm bacterium (any class, order,family, genus, species or strain disclosed above) according to the invention is 160 mM to 200 mM, and / or the minimum MIC is at least 160 mM, preferably at least 180 mM, preferably about 200 mM, (l) The MIC range of N,2-dimethylpropan-1-amine for the mutated diderm bacterium (any class,order, family, genus, species or strain disclosed above) according to the invention is 40 mM to 80 mM, and / or the minimum MIC is at least 40 mM, preferably at least 60 mM, preferably about 80 mM ,(m) The MIC range of N-ethylcyclohexanamine for the mutated diderm bacterium (any class,order, family, genus, species or strain disclosed above) according to the invention is 40 mM to 80 mM, and / or the minimum MIC is at least 40 mM, preferably at least 60 mM, preferably about 80 mM, or (n) any combination of (a) to (n), for example the combinations of:o (a), (b) and (c), oro all of (a) to (m).METHOD FOR OBTAINING THE MUTATED BACTERIUM The mutated bacterium according to the invention may be obtained by a method comprising: a) growing a reference bacterium in continuous culture under turbidostat regime in a permissivemedium comprising a permissive concentration Cp of an amine compound equal to its minimum inhibitory concentration (MIC) for the reference bacterium minus 10-20% (MIC-10- 20%) for one to five days (preferably for three or four days); b) growing the bacterial population obtained at the end of step a), using:(i) turbidostat regime with gradual increase from Cp of the concentration of the aminecompound, until the bacterial population grows in a stressing medium comprising astressing concentration Cs of amine compound, wherein the Cs is preferably equalto 1.2xCp (1.2 times Cp), preferably 1.5xCp, more preferably 2xCp, more preferably at least 2xCp (or wherein the Cs is preferably about 1.2xCp, preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp); and / or (ii) medium swap regime using:^ a permissive medium comprising a permissive concentration of the aminecompound equal to Cp, and^ a stressing medium comprising a stressing concentration Cs of the aminecompound, wherein the Cs is preferably equal to 1.2xCp (1.2 times Cp), preferably 1.5xCp, more preferably 2xCp, more preferably at least 2xCp (or wherein the Cs is preferably about 1.2xCp, preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp), until the proportion of dilutions with the stressing medium reaches 100%; c) optionally growing the bacterial population obtained at the end of step b) under turbidostatregime for one to five days (preferably for three days) in a medium comprising a concentrationof the amine compound equal to Cs; d) selecting the best growing bacterial isolate; ande) optionally, repeating steps a) to d) using the best growing bacterial isolate as a new referencebacterium, except that: (i) the same amine compound is used and the new Cp in repeated step a) is equal to Cs inthe previous step c), or (ii) another amine compound is used and Cp in repeated step a) is equal to the MIC of theother amine compound for the new reference bacterium minus 10-20%. In step a), a reference bacterium (any class, order, family, genus, species or strain disclosed above, notably Escherichia coli strain BL21(DE3)) is grown under turbidostat regime in a permissive medium comprising a permissive concentration Cp of an amine compound. The permissive concentration Cpof the amine compound is slightly lower than the MIC of the amine compound for the referencebacterium, equal to MIC – 10-20%. The duration of step a) is one to five days, preferably three or fourdays. In step b), tolerance for the amine compound is increased by growing the bacterial cell population obtained at the end of step a) for one to ten days (preferably for 2 to 7 days) in increasing concentrations of the amine compound. The concentrations may be increased using two distinct strategies. In a first strategy, turbidostat regime is used, the concentration in the amine compound being increased regularly from permissive concentration Cp to a stressing concentration Cs (stressing refers to the fact that this concentration would be stressing for the bacterial cell population obtained at the end of step a), although it is normally no more stressing when this concentration is reached in thefirst strategy). The rate of increase in the concentration of the amine compound is selected so thatsufficient bacterial growth is maintained. In a second strategy, the concentration in the amine compound is not increased regularly. Instead, a medium swap regime (WO2003004656A1; Marliere et al., 2011) is used, which is based on the use of two distinct media comprising distinct concentrations of the amine compound:^ a permissive medium comprising a permissive concentration of the amine compound equalto Cp, and^ a stressing medium comprising a stressing concentration Cs of the amine compound, whereinthe Cs is preferably equal to 1.2xCp (1.2 times Cp), preferably 1.5xCp, more preferably 2xCp, more preferably at least 2xCp (or wherein the Cs is preferably about 1.2xCp,preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp).Medium swap regime enables gradual adaptation of a bacterial population to grow in a non-permissiveor stressing medium. The growing culture can be diluted by either permissive or stressing medium. The choice between the two dilution media depends on the turbidity of the culture with respect to aset optical density (OD) threshold (e.g., OD at 600 nm value of 0.4, preferably an OD at 600 nm valueof 0.5, preferably an OD at 600 nm value of 0.6, more preferably OD at 600 nm value of 0.7). When the measured OD exceeds the threshold, a pulse of stressing medium is injected; otherwise a pulseof permissive medium is injected. Dilutions are triggered every 5 to 15 minutes (preferably every 10minutes) with a fixed volume of medium, thus imposing a generation time (i.e. the time required fora cell population to double in number) on the cell population. The medium swap regime is maintained until the proportion of dilutions with the stressing mediumreaches 100%, which may take 1 to 10 weeks, preferably 2 to 8 weeks, depending notably on theselected Cs concentration. Systems permitting turbidostat regime and medium swap regime are disclosed in WO2000 / 034433 andnotably include for example the GENEMAT automated continuous culture device (available fromGinkgo Bioworks), or the automated culture devices available from Chi.Bio (the open-source roboticplatform for experimental automation in biological science research). Step c) is intended to stabilize and lower the generation time of the bacterial population obtained atthe end of step b). In step c), the bacterial population is grown under turbidostat regime for one tofive days (such as 1, 2, 3, 4 or 5 days, preferably for three days) in a medium comprising a concentration of the amine compound equal to Cs. In all of steps a) to c), the culture medium, to which the amine compound is added, is selected depending on the reference bacterium used, in order to promote optimal growth of the referencebacterium. For instance, when the reference bacterium is an Escherichia strain, and more particularlyan E. coli strain (in particular E. coli strain BL21(DE3)), the culture medium may be MS-glucose culturemedium (pH 7.2) (which contains 4 mM citric acid, 1 mM MgSO4, 20 mM NH4Cl, 50 mM K2HPO4, 0.2% w / v d-glucose, and 0.1% v / v trace elements mix). A skilled person will know appropriate culture media for other types of reference bacteria. In step d), the best growing bacterial isolate from the bacterial population obtained at the end of step c) is selected. Selection may be performed by growing the stabilized bacterial population obtained at the end of step c) in solid medium comprising a concentration of the amine compound equal to Cs, and subsequently inoculating isolated colonies into liquid medium comprising varied concentrations of the amine compound equal to Cs, and Cs minus 10-20%, and Cs plus 10-20%. When a further increase in tolerance to the same amine compound (and optionally to other amine compounds) is desired, steps a) to d) can be repeated, using in repeated step a) the best growing bacterial isolate as a new reference bacterium and a new Cp concentration equal to Cs in previous step c). Alternatively, one can use in repeated step a) the best growing bacterial isolate as a new reference bacterium, another amine compound, and a new Cp concentration equal to the MIC of the other aminecompound for the new reference bacterium minus 10-20%. In this case, the method contains anadditional step d1), in which the MIC of the other amine compound for the new reference bacterium is determined. PREFERRED MUTATED BACTERIA ACCORDING TO THE INVENTIONParticularly preferred mutated diderm bacteria according to the invention may be selected from thegroup consisting of: i. a mutated bacterium of the strain JHX 1.2.3 (also called G5847), deposited under theprovisions of Budapest treaty, at the Collection Nationale de Cultures de Microorganismes (CNCM, having the address: CNCM, Institut Pasteur, 25 rue du Docteur Roux, F-75724 Paris Cedex 15), on 31 January 2024, under the deposit number CNCM I-6031; and ii. a mutated bacterium of the strain JHX 4.2.8 (also called G6180), deposited under theprovisions of Budapest treaty, at the Collection Nationale de Cultures de Microorganismes (CNCM, having the address: CNCM, Institut Pasteur, 25 rue du Docteur Roux, F-75724 Paris Cedex 15), on 31 January 2024, under the deposit number CNCM I-6032.These mutated bacteria have increased tolerance to rac-2-aminohexane, rac-2-aminoheptane, and cyclohexylamine compared to the reference bacterium from which they have been derived (E. colistrain BL21(DE3), see Example 1 and Figure 3), and strain JHX 4.2.8 has been further demonstratedto have increased tolerance to further amine compounds (those disclosed in Table 4 above, seeExample 1 and Table 5 below).IN VITRO METHODS AND USESThe mutated diderm bacteria according to the invention have increased tolerance to various amine compounds. Indeed, even when selecting a mutant using only one amine compound, the inventors found that the selected mutant was in fact tolerant to increased concentrations of many distinctamine compounds. As such, they can be used for any purpose involving the culture of bacteria in a medium comprising elevated concentrations of one or more amine compounds. Such uses include, without being limited to: the transformation (preferably the biotransformation) of amine compounds, or the production (preferably the bioproduction) of amine compounds, or any combination thereof.The present invention thus also relates to an in vitro use of the mutated bacterium according to theinvention, for the transformation (preferably the biotransformation) of amine compounds, or for the production (preferably the bioproduction) of amine compounds, or any combination thereof; wherein the amine compound is preferably selected from the group consisting of a compound of formula (Formula I);wherein :c) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, said groups being optionally substituted,with proviso that R1 and R2 are not both H, ord) R1 and R2 form together a saturated or non-saturated ring optionally substituted and / oroptionally fused with another ring,And wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl, said groups beingoptionally substituted.The present invention also relates to an in vitro method for the transformation (preferably thebiotransformation) of amine compounds, for the production (preferably the bioproduction) of amine compounds, or any combination thereof; comprising using the mutated bacterium according to the invention; wherein the amine compound is preferably selected from the group consisting of a compound of formula (Formula I);wherein :c) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, said groups being optionally substituted,with proviso that R1 and R2 are not both H, ord) R1 and R2 form together a saturated or non-saturated ring optionally substituted and / oroptionally fused with another ring,And wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl, said groups beingoptionally substituted.When the in vitro use or the in vitro method according to the invention is for the production(preferably bioproduction) of amine compounds, the substrate may be a carbonyl compound.In the in vitro use or the in vitro method according to the invention, the mutated bacterium preferablyexpresses, or is modified to express, an enzyme having an activity of transformation (preferably the biotransformation) of amine compounds, of production (preferably bioproduction) of amine compounds, or any combination thereof.In this case, the activity of the enzyme is preferably selected from the group consisting of: aminedehydrogenase (AmDH), reductive aminase (RedAm), transaminase (or aminotransferase), amine oxidase, amine-degrading activity, opine dehydrogenase, imine reductase, and ammonia lyase (Parmeggiani et al., 2018; Sangster et al., 2020; Ducrot et al., 2021).Amine dehydrogenase (AmDH) enzymes (EC 1.4.1.-) catalyze the NAD(P)H-dependent reductiveamination of ketones and aldehydes to chiral amines with ammonia as the preferred amine donor.They are notably useful in the biotransformation of ketone and aldehydes into chiral amines or in the bioamination of alcohol when used in combination with an alcohol dehydrogenase (ADH). They are either derived from amino-acid dehydrogenases by protein engineering (examples : Ch1-AmDHengineered from LeuDH GenBank: AAA22570.1 and PheDH GenBank: BAA08816.1; BhAmDH-E113D / N276L engineered from PheDH GenBank: BAB03937.1)) or from the native AmDH family andengineered-protein derived (examples CfusAmDH GenBank: EPX55364.1, MsmeAmDH GenBank: SUA34519.1).Transaminase (also referred to as aminotransferase) enzymes (TA) are reversible enzymes whichtransfer an amino group from an amino donor to a ketone or aldehyde. They require pyridoxal phosphate as coenzyme or cofactor, the amino group is converted into a ketone in the deamination reaction and vice versa in the amination reaction. ω-transaminases (ω-TA) accept in principle any ketone or amine in opposite to TA which act on a carbonyl with a carboxylic acid group in the α position. One example is the engineering of ATA-117 for the industrial synthesis of Januvia®(sitagliptin phosphate). Amine oxidase enzymes are oxidoreductases (EC 1.4.3.4.). Enzymes of this class catalyse redox reactions, in particular monoamine oxidases (MAOs) are able to oxidize amines to imines withsimultaneous reduction of oxygen to hydrogen peroxide. One example is the MAO from the fungusAspergillus niger (MAO-N) (GenBank: AAA98490.1).Other reductases : bioreductive aminations. N-methyl amino acid dehydrogenases (NMAADHs / DpkAs),ketimine reductases (KIREDs), and pyrroline-5-carboxylate reductases (P5CRs) have recently been thefocus of research for bioreductive aminations, where various enzymes from these families may beused to access a series of N-alkylated amino acids. For example, the DpkA from Pseudomonas putida(GenBank: BAD89743.1) may be used to generate a range of N-alkylated glycine derivatives.Opine dehydrogenase enzymes (OpDHs) are a class of oxidoreductases that catalyse the reductiveamination of α-keto acids with α-amino acids, using NADH as cofactor. Some have been engineeredto couple ketones with amines to form various amines (example : the evolution of CENDH GenBank:BAA08145.1). Imine reductase enzymes are NADPH-dependent oxidoreductases that have been shown to catalyse the asymmetric reduction of pre-formed prochiral imines. In presence of excess amine donor, somecan perform the reductive amination of ketones (example : (R)-IRED-Sr GenBank: ACZ83929.1).Reductive aminase (RedAm) enzymes are a subpart of IRED enzyme family that are able to catalysethe imine formation step in addition to its reduction (example : AspRedAm GenBank: BAE66526.1).Ammonia lyase enzymes (EC 4.3.1.5) perform enzymatic hydroaminations of alkenes. They catalyse the reversible addition of ammonia across C=C-double bonds of α,β-unsaturated carboxylic acids. Thereaction is stereoselective and leads to the formation of chiral α-amino acids and a large excess ofammonia is necessary. The phenylalanine ammonia lyases (PAL) from Anabaena variabilis (GenBank:ABA23593.1) is an example.DESCRIPTION OF THE FIGURES Figure 1. (A) First adaptation of E. coli BL21 (DE3) wild-type strain to growth in the presence of rac- hexan-2-amine (30 mM) via directed evolution in continuous culture. (B) Adaptation of isolate JHX 1.2.3 to growth in the presence of rac-hexane-2-amine (100 mM) via directed evolution in continuous culture. In (A–B) dot curves show the average daily generation time, while triangle curves show the ratio of the daily number of diluting pulses with stressing medium to the total number of diluting pulses. In (A–B) grey and light grey areas indicate periods of cultivation under turbidostat and medium swap regime, respectively; additionally, areas with diagonal stripes indicate the days in which the cultivation regime was changed. During periods of cultivation under medium swap regime, a generation time of 3 h 10 min and 2 h 20 min, in (A) and (B) respectively, was set by the volume of the medium pulses injected at regular time intervals (every 10 min). Note: in (A), given the short period of cultivation under medium swap regime, the average daily generation time on day 5 waslower than 3 h 10 min. However, 3 h 10 min was the effective generation time imposed by the fixeddilution rate during medium swap cultivation. Isolated adapted strains are shown with vertical arrows.Figure 2. Plate reader growth profile of strain E. coli BL21 (DE3) and of isolates JHX 1.2.3 and JHX4.2.8 in MS-glucose medium containing rac-hexan-2-amine (30, 100 mM) during incubation at 37 °C and constant agitation. Each curve represents the average of three independent measurements.Figure 3. Minimum inhibitory concentration (MIC) assays on E. coli cells using rac-hexan-2-amine,rac-heptan-2-amine, and cyclohexylamine measured in MS-glucose after incubation at 37 °C and 150 rpm for 18 h. These amines exhibited toxicity at low or moderate concentration on the E. coli BL21 (DE3) strain. Each compound was tested in triplicate with consistent results.Figure 4. (A) Bioamination of hexan-2-one, heptan-2-one and 1-(4-fluorophenyl)propan-2-one (PFPA)(50–300 mM) by E. coli resting cells (60 mg mL−1, cell wet weight) co-expressing Ch1-AmDH and Cb-FDH in aqueous HCOONH4 / NH4OH (1 M, pH 8.5). (B) Same as in (A), with addition of NAD+ (1 mM). (C) Bioamination of hexan-2-one (20–50 mM) by combing E. coli resting cells expressing Ch1-AmDH (60 mg mL−1, cell wet weight) with varied loadings of resting cells expressing Cb-FDH (10–40 mg mL−1, cell wet weight) in aqueous HCOONH4 / NH4OH (1 M, pH 8.5) In (A–C), reaction volume 1 mL; incubation at 30 °C and 170 rpm for 24 h (black: BL21 (DE3) cells; light grey: JHX 4.2.8 cells). Error bars in (A– C) indicate the standard deviation of three independent experiments. EXAMPLES Although the present invention herein has been described with reference to particular embodiments, it is to be understood that these embodiments are merely illustrative of the principles and applications of the present invention. It is therefore to be understood that numerous modifications may be made to the illustrative embodiments and that other arrangements may be devised without departing from the spirit and scope of the present invention as defined by the appended claims. 1. EXAMPLE 1: GENERATION OF NOVEL STRAINS 1.1 Materials and Methods 1.1.1. General presentation of the Method Chemical compounds that are not natural intermediates of cellular metabolism might impact adversely cellular processes. Toxicity can result from the chemical reactivity or the physico-chemical properties of the compounds and can cause targeted or unspecific deleterious effects. The mechanisms by which amines interfere with E. coli metabolism are not known. In order to increase the tolerance of E. coli cells to amines, we resorted to adaptive evolution protocols using the GENEMATtechnology for automated continuous culture (WO2000 / 034433) with the objective of obtaining mutant E. coli able to withstand high concentrations of amines. The phenotype of isolated adapted strains was characterized in terms of growth profile, amine tolerance, survivability, genome sequence. The biocatalytic performance of the adapted cell transformed with recombinant plasmids encoding for AmDH activity was contrasted to that of the wild-type, demonstrating the occurrence of more robust in vivo biocatalysis and higher amine titers. Adaptative directed evolution experiments were conducted in the automated self-cleaning GENEMAT devices developed by the French Alternative Energies and Atomic Energy Commission (CEA) in collaboration with the society ALTAR. The volume of the culture is maintained constant (16 mL at 37 °C) by diluting it with a pulse of fresh medium and discarding the same volume of used culture. Two growth regimes were used: turbidostat and medium swap. In the former case, the dilution rate was dependent on the cell growth and the dilutions with fresh medium (1.6 mL pulse) occurred when the optical density threshold was exceeded. In the latter case, the medium to dilute “swapped” between a stressing (high amine concentration) and permissive one (low amine concentration corresponding at a concentration just below the MIC (see below) of the amine for wild type strain BL21(DE3)) depending on whether the measured optical density threshold is exceeded or not, respectively. Under medium swap regime, the dilution rate was fixed thus imposing a generation time on the culture. Once the proportion of dilutions with stressing medium reached 100%, the evolved population growing in the stressing medium conditions was then stabilized and improved to decrease its generation time under turbidostat regime. The best growing isolate obtained from the later population was used to inoculate a second continuous culture for further adaptation with a stressing medium containing even higher amine concentration. From this second round of adaptation, the best growing isolate was selected and its genome sequenced to identify the mutations which were fixed during the evolution process from the wild type strain. Following transformation with a recombinant plasmid encoding the desired amine-forming enzymes, the adapted strain was used as biocatalyst for biotransformation of ketone substrates into amines. As a consequence of acquired higher tolerance, the cell survival rate was improved in the conditions of biotransformation in comparison with non-evolved strain. Advantages: Tolerance to amines acquired by the fixation of spontaneous beneficial mutations in the genome. Stability of the phenotype (tolerance to amines). Higher tolerance allows for extended maintenance of metabolically active cells for the production of enzymes and cofactors, hence for higher biotransformation yield. The evolved tolerance toward one amine rendered the cell tolerant to other amines, which widens the applications. Another advantage of this method compared to physical protection of the biocatalytst, is that operational conditions to run the biotransformation remain common ones. Experimenters do not need to take precautions to verify that the biocatalyst formulation is correct. It ensures reproducibility and can be applied to different biotransformations by inserting the desired genes. 1.2. Results Using the GENEMAT automated continuous culture device, the first adaptation of E. coli BL21 (DE3) was initiated with a continuous culture in MS-glucose medium containing 15 mM of rac-2-aminohexane growing in turbidostat regime (Figure 1a), where the dilution rate was dependent on the cell growth and the culture was automatically diluted with fresh medium every time a fixed cell density threshold (OD 600 nm value of 0.4) was exceeded. This experimental strategy enabled the selection of faster growing cells (generation time 1 h 35 min, cultivation day 3). To further increase the tolerance to rac-2-aminohexane, the cell population was subsequently switched to conditional medium swap regime for gradual adaptation to growth in stressing medium containing 30 mM of rac-2-aminohexane (Figure 1a). The permissive medium contained 15 mM of rac-2-aminohexane and, consequently, the lowest tolerable concentration of rac-2-aminohexane was maintained over passing generations. After 6 days of cultivation in conditional medium swap regime, the proportion of dilutions with stressing medium rose until reaching 100% (Figure 1a), indicating that the E. coli population grows in MS- glucose with 30 mM of rac-2-aminohexane. To stabilize and lower the generation time of the population (1 h 10 min, cultivation day 9), the adapting cells were ultimately grown in stressing medium under turbidostat regime (Figure 1a). The best growing isolate obtained from the later population on solid MS-glucose medium was utilized to inoculate a second continuous culture for further adaptation to rac-2-aminohexane. The cells were grown under turbidostat regime in MS-glucose with 30 mM of rac-2-aminohexane until day 3 (Figure 1b). From day 3 to day 10, the adaptingcells were cultivated in a conditional medium swap using MS-glucose with 30 and 100 mM of rac-2- aminohexane as permissive and stressing medium, respectively. On day 10, after ca. 60 generations in medium swap regime, the maximum proportion of dilutions with stressing medium (i.e., 100%) was reached (Figure 1b). Lastly, a period of cultivation in turbidostat regime was employed to consolidate the population, leading to a generation time of 1 h 11 min at the end of the adaptation (day 16). Fiveisolates from the later population were selected on solid MS-glucose medium containing 100 mM ofrac-2-aminohexane, and subsequently inoculated into liquid MS-glucose medium containing varied concentrations of rac-2-aminohexane (80–100 mM). The best growing isolate (strain JHX 4.2.8) was selected. We characterized the growth phenotype of the isolated JHX 4.2.8 in MS-glucose medium containingrac-2-aminohexane. Figure 2 shows that the two isolates tested, i.e. JHX 1.2.3 (also called G5847)and JHX 4.2.8 (also called G6180), grow in the presence of rac-2-aminohexane (30 mM) whereas BL21(DE3) wild-type does not. By contrast, only strain JHX 4.2.8 grew with 100 mM of rac-2-aminohexane.Tolerance of the strains JHX 1.2.3 and JHX 4.2.8 for rac-2-aminohexane and two related compoundswas monitored and compared to the unevolved strain BL21 (DE3) through minimum inhibitory concentration (MIC) assays (Figure 3). We defined the MIC as the lowest amine concentration that precludes visible cell growth in MS-glucose medium after 18 h of incubation. The strains were inoculated in MS-glucose medium and cultured overnight at 37 °C and 150 rpm. The following day, a series of culture tubes containing MS-glucose medium and the compound to be tested at variedconcentrations was inoculated with the pre-cultures to obtain an initial OD 600 nm of 0.6. The tubeswere inoculated with 30 μL of culture within the above-mentioned optical density range and incubated for 18 h at 37 °C and 150 rpm.Strain JHX 1.2.3 displayed a superior tolerance to rac-2-aminohexane (compound 1 in Table 4 above)(MIC = 46 mM), rac-2-aminoheptane (compound 2 in Table 4 above) (MIC = 22 mM) and cyclohexylamine(compound 3 in Table 4 above) (MIC = 52 mM) compared to the non-evolved E. coli strain BL21 (DE3)(see Figure 3). Strain JHX 4.2.8 displayed a further increased tolerance to rac-2-aminohexane 1 (MIC = 96 mM)compared to the non-evolved E. coli strain BL21 (DE3) (MIC = 16 mM), which amounted for an overallsix-fold MIC increase. In addition, the JHX 4.2.8 adapted strain was four to five times more tolerant to rac-2-aminoheptane 2 and cyclohexylamine 3 with MIC values of 40 and 134 mM respectively,compared to 22 and 52 mM for the non-evolved E. coli strain BL21 (DE3), respectively (see Figure 3).The tolerance of strain JHX 4.2.8 was compared to that of the non-evolved E. coli strain BL21 (DE3)for further amine compounds (compounds 4 to 13 of Table 4 above) through minimum inhibitoryconcentration (MIC) and MIC range assays.Results are presented in Table 5 below and confirm that strain JHX 4.2.8 tolerates significantlyincreased concentrations of many distinct amine compounds compared to the non-evolved E. coli strain BL21 (DE3).Table 5. Tolerance of strain JHX 4.2.8 and the non-evolved E. coli strain BL21 (DE3) to aminecompounds 4 to 13 disclosed in Table 3 above.* For all compounds except those with ** or ***,measurement was performed after 18 h of incubation. ** Measure was performed after 24 h of incubation. *** Measurement was performed after 48 h of incubation: Amine compound number in MIC range (mM)* previous Table 4 WT JHX 4.2.8 (E. coli strain BL21 (DE3))4 10-20 20-405 10-20 40-806 5-10 40-807 0-5 10-208 80-160 >1609 80-160 >16010 160-200 200-25011** 80-160 >16012*** 20-40 40-8013 20-40 40-802. EXAMPLE 2: GENOME SEQUENCING OF NOVEL STRAINS2.1. Materials and MethodsThe genomic DNA of the non-evolved parent strain Escherichia coli BL21 (DE3) and of the evolvedisolate JHX4.2.8 was purified using the Genomic DNA extraction kit from QIAGEN following the manufacturer’s protocol. 1 µg of purified genomic DNA was provided to Novogene (UK) Company Limited (Cambridge, UK), who performed the preparation of pair-end libraries (2x150 base pairs) and Illumina sequencing ensuring a sequencing depth of 100x. The PALOMA pipeline integrated in thebioinformatics platform MicroScope http: / / www.genoscope.cns.fr / agc / microscope , was used to mapthe reads against the E. coli B21 (DE3) strain reference sequence (NC_012971.2). The sequence reads from the genomic library of the strain JHX4.2.8 were compared to those of the non-evolved parent strain for detecting single nucleotide variations, short insertions or deletions (in / dels), as well as read coverage variations. 2.2. ResultsCompared to the genome of the non-evolved E. coli strain BL21 (DE3), 21 mutations were identifiedin the genome of strain JHX4.2.8 in genes classified in eggnog v5 nomenclature under various functional categories, encoding proteins involved in: ^energy production and / or energy conversion (eggNOG v5 category C),^ cell cycle control, cell division, chromosome portioning (eggNOG v5 category D),^ nucleotide transport and / or nucleotide metabolism (eggNOG v5 category F),^ carbohydrate transport and metabolism (eggNOG v5 category G),^ lipid transport and metabolism (eggNOG v5 category I),^ translation, ribosomal structure and biogenesis (eggNOG v5 category J),^ transcription (eggNOG v5 category K),^ cell wall / membrane / envelope biogenesis (eggNOG v5 category M),^ signal transduction mechanisms (eggNOG v5 category T),^ intracellular trafficking, secretion, and vesicular transport (eggNOG v5 category U),^ inorganic ion transport and / or inorganic ion metabolism (eggNOG v5 category P),^ function unknown (eggNOG v5 category S ) : including gene yjgL (GenBank identificationnumber for Escherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_04119), and gene yqjA (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_02964). Three mutations in intergenic regions were further identified.The identified mutations are listed in Table 3 above. 3. EXAMPLE 3: BIOTRANSFORMATION 3.1. Materials and Methods E. coli strains carrying plasmids for amine dehydrogenase activity were precultured overnight at 37 °C and 150 rpm in "Lysogeny Broth" medium (LB medium, also known as Luria–Bertani medium; ) Bertani, 2004). Fresh LB medium was inoculated with the overnight culture at 1:100 dilution and grown at 37 °C and 150 rpm until reaching an OD 600 nm between 0.6 and 0.9. Recombinant protein expression was induced by addition of 0.5 mM IPTG followed by cultivation at 25 °C and 150 rpm for additional 18 h. Cells were harvested by centrifugation, washed with reaction buffer, and re- suspended in reaction buffer to the adequate concentration (in cell wet weight per mL). Biotransformations were performed in 1 M HCOONH4 / NH4OH (pH 8.5, final volume 1 mL) containing the adequate concentration cells and the specified concentration of ketone. Biotransformations were incubated at 30 °C and 170 rpm for 24 h. Work-up was initiated by quenching the reactions with 10 M KOH (200 μL), followed by extraction with ethyl acetate (2 × 500 μL). The combined organic phases were dried over MgSO4 anhydrous, and the conversion was calculated based on the areas of substrate and product as determined by gas chromatography. 3.2. Results One application of E coli strains more tolerant to amines is the biotransformation of ketones into (chiral) amines, using cells transformed with recombinant plasmids encoding Amine Dehydrogenaseactivity. We applied the non-evolved E. coli strain BL21 (DE3) and the evolved strain JHX 4.2.8 forthe biotransformation of 2-hexanone, 2-heptanone and para-fluorophenylacetone (PFPA). With E. coli strains co-expressing the chimeric amine dehydrogenase Ch1-AmDH (Bommarius et al., 2014 ; Knaus et al., 2017) and the formate dehydrogenase Cb-FDH (Schütte, 1976), conversions at 100 mM of 2-hexanone was 75% with evolved resting cells versus 25% with wild-type (E. coli strain BL21 (DE3)) ones(Figure 4A). With addition of external NAD+, the conversion of PFPA was nearly quantitative at 200 mM with strain JHX 4.2.8 compared to 35% with wild-type (Figure 4B). By combining E. coli resting cells expressing AmDH with cells expressing FDH activity, the differences between wild-type strains and evolved ones were even higher (Figure 4C). BIBLIOGRAPHIC REFERENCES Ducrot, L., Bennett, M., Grogan, G. & Vergne-Vaxelaire, C. NAD(P)H-dependent enzymes for reductiveamination: Active site description and carbonyl-containing compound spectrum. Adv. Synth. Catal. 363,328–351 (2021). Mutti, F.,Knaus, T. Chapt. 6 Enzymes Applied to the Synthesis of Amines, Ed. De Gonzalo, G. andLavandera, I., Biocatalysis for Practitioners: Techniques, Reactions and Applications. Wiley (2021).Slabu, I.; Galman, J. L.; Lloyd, R. C.; Turner, N. J., Discovery, Engineering, and Synthetic Application ofTransaminase Biocatalysts. ACS Catal. 7 (12), 8263-8284 (2017).Klatte, S., Lorenz, E., Wendisch, V. F., Whole cell biotransformation for reductive amination reactions.Bioengineered, 5, 56-62 (2014).B. Lin, Y. Tao, Whole-cell biocatalysts by design. Microbial Cell Factories, 16, 106 (2017).Houwman, J. A., Knaus, T., Costa, M., Mutti, F. G., Efficient synthesis of enantiopure amines from alcoholsusing resting E. coli cells and ammonia. Green Chem., 21, 3846-3857 (2019)Sun, Z., Hübner, R., Li, J. Wu, C. Artificially sporulated Escherichia coli cells as a robust cell factory forinterfacial biocatalysis. Nat. Comm.13, 3142 (2022).Gao,L., Feng, L., Sauer, D. F., Wittwer, M., Hu, Y., Schiffels, J., Li, X., Cell Rep. 3, 101054 (2022)Bommarius, B. R., Schurmann,M., Bommarius, A. S. A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes. Chem. Commun. 50, 14953–14955 (2014);Knaus, T., Böhmer, W., Mutti, F. G., Amine dehydrogenases: efficient biocatalysts for the reductiveamination of carbonyl compounds. Green Chem. 19, 453-463 (2017)Schütte, H., Flossdorf, J., Sahm, H., Kula, M.-R., Purification and Properties of Formaldehyde Dehydrogenase and Formate Dehydrogenase from Candida boidinii. Eur. J. Biochem.62, 151-160 (1976) Marlière, P., Patrouix, J., Döring, V., Herdewijn, P., Tricot, S., Cruveiller,S., Bouzon, M., Mutzel, R.,Chemical Evolution of a Bacterium’s Genome. Ang. Chem. Int.Ed. 50, 7109-7114 (2011);WO2000 / 034433Jeong H et al. 2009. Genome sequences of Escherichia coli B strains REL606 and BL21(DE3). J MolBiol 394:644–652Mairhofer et al., 2014. Finished Genome Sequence of Escherichia coli K-12 Strain HMS174 (ATCC 47011) (PMID: 25414489)Parmeggiani, F., Weise, N.C., Ahmed, S. T., Turner, N. J. Synthetic and Therapeutic Applications ofAmmonia-lyases and Aminomutases. Chem. Rev. 118, 1, 73–118 (2018)Sangster J. J., Marshall J. R., Turner N. J., Mangas-Sanchez J. New Trends and Future Opportunities in the Enzymatic Formation of C-C, C-N, and C-O bonds. Chembiochem.18;23(6):e202100464 (2022).

Claims

CLAIMS1. A mutated bacterium tolerant to elevated concentrations of one or more amine compound(s), themutated bacterium being derived from a reference bacterium by insertion of one or more mutations in its genome, wherein the bacterium is a diderm bacterium, and wherein:- at least one mutation occurs in a gene selected from the group consisting of:(i) genes encoding proteins involved in lipid transport and / or lipid metabolism;(ii) genes encoding proteins involved in carbohydrate transport and / or carbohydrate metabolism;(iii) genes encoding proteins involved in nucleotide transport and / or nucleotide metabolism;(iv) genes encoding proteins involved in energy production and / or energy conversion;(v) genes encoding proteins involved in cell cycle control, cell division, chromosome partitioning,and any combination thereof; (vi) genes encoding proteins involved in translation, ribosomal structure ribosomal biogenesis,and any combination thereof; (vii) genes encoding proteins involved in transcription;(viii) genes encoding proteins involved in cell wall biogenesis, cell membrane biogenesis,cell envelope biogenesis, and any combination thereof; (ix) genes encoding proteins involved in intracellular trafficking, secretion, vesicular transport,and any combination thereof; (x) genes encoding proteins involved in signal transduction mechanisms;(xi) genes encoding proteins involved in inorganic ion transport and / or inorganic ion metabolism;(xii) the gene yjgL (GenBank identification number for Escherichia coli strain BL21(DE3):CP001509.3, locus tag : ECD_04119); (xiii) the gene yqjA (GenBank identification number for Escherichia coli strain BL21(DE3) :CP001509.3, locus tag : ECD_02964) ; and(xiv) any combination of (i) to (xiii); and / or- at least one mutation occurs in an intergenic region, wherein the intergenic region is preferablyselected from the group consisting of :(i) the intergenic region located between gene paoA (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00245) and gene yagU (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00246), (ii) the intergenic regions located between gene yfgO (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02385) and gene bepA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02386), (iii) the intergenic regions located between gene rluD (GenBank identification number forEscherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02484) and gene bamD(GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_02485), and (iv) any combination thereof.

2. The mutated bacterium according to claim 1, wherein the amine compound(s) is(are) selected from the group of amine compounds of formula (I):wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, with proviso that R1 and R2 are notboth H, or b) R1 and R2 form together a saturated or non-saturated ring optionally fused with another ring,and wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl.

3. The mutated bacterium according to claim 2, wherein the amine compound(s) is(are) selected from the group of amine compounds of formula (I):Wherein R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxyalkyl, aryloxy alkyl, and alkanoyl alkyl, with proviso that R1 and R2 are not both H, andwherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl.

4. The mutated bacterium according to claim 1, wherein:a) R1 and R2 are independently selected from the group consisting of H, C1-C10 alkyl, C1-C10heteroalkyl, C2-C10alkenyl, C6-C12aryl, C4-C12heteroaryl, C6-C14heretoaryl alkyl, C7-C14arylalkyl, C8- C14aryl alkenyl, C2-C10alkyloxy alkyl, C7-C14aryloxy alkyl, C5-C14heteroaryloxy alkyl and C2-C10alkanoyl alkyl; or b) R1 and R2 form together a saturated or unsaturated 4-7-member ring optionally fused to another 4-7-member ring.

5. The mutated bacterium according to claim 1, wherein the one or more amine compound is selected from rac-2-aminohexane, rac-2-aminoheptane, cyclohexylamine, furfurylamine, 1-phenylethan-1- amine, n-hexyamine, 5-methylhexan-2-amine, 4-phenyl-2-butylamine, 3-pentylamine, 2-butylamine,but-3-en-1-amine, 2-aminopropan-1-ol, N,2-dimethylpropan-1-amine, N-ethylcyclohexanamine, and any combination thereof.

6. The mutated bacterium according to any one of claims 1 to 5, wherein the diderm bacteriumbelongs to the Gammaproteobacteria class, preferably to an order selected from the group consistingof: -the Enterobacterales order,- the Pseudomonadales order,- the Acidiferrobacteraless order,- the Aeromonadales order,- the Alteromonadales order,- the Arenicellales order,- the Candidatus Comchoanobacterales order,- the Candidatus Competibacterales order,- the Candidatus Foliamicales order,- the Candidatus Porifericomitales order,- the Candidatus Rariloculales order,- the Candidatus Spongiifermentumdales order,- the Candidatus Tethybacterales order,- the Cardiobacteriales order,- the Cellvibrionales order,- the Chromatiales order,- the Immundisolibacterales order,- the Kangiellales order,- the Legionellales order,- the Methylococcales order,- the Moraxellales order,- the Nevskiales order,- the Oceanospirillales order,- the Orbales order,- the Pasteurellales order,- the Salinisphaerales order,- the Thiohalobacterales order- the Thiohalomonadales order- the Thiohalorhabdales order- the Thiohalospirales order- the Thiotrichales order,- the Vibrionales order, and- the Xanthomonadales order.

7. The mutated bacterium according to any one of the preceding claims, wherein the gene encodingproteins involved in energy production and / or energy conversion is selected from the group consistingof: narG (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag: ECD_01202), nuoC (GenBank identification number for Escherichia coli strain BL21(DE3) :CP001509.3, locus tag : ECD_02211), and any combination thereof;wherein the mutation is preferably located at a position, in the genome of the mutated bacterium, as defined below: -narG (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_01202) : a position in the genome of the mutated bacterium equivalent to position1271070 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; nuoC (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_02211) : a position in the genome of the mutated bacterium equivalent to position2289710 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; or- any combination thereof.

8. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in cell cycle control, cell division, chromosome partitioning, and any combination thereof, is etk (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_00984), wherein the mutation is preferably located at a position in the genome of the mutated bacteriumequivalent to position 1047795 in the genome of E. coli strain BL21(DE3), after optimal globalalignment of both genomes.

9. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in nucleotide transport and / or nucleotide metabolism is selected from the group consisting of speD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00119), pgi (GenBank identification number for Escherichiacoli strain BL21(DE3): CP001509.3, locus tag: ECD_03897), andany combination thereof,wherein the mutation is preferably located at a position, in the genome of the mutated bacterium,as defined below: -speD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00119) : a position in the genome of the mutated bacterium equivalent to position137789 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 598 inthe speD gene at locus ECD_00119), after optimal global alignment of both genomes;- pgi (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03897): a position in the genome of the mutated bacterium equivalent to position4142045 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 917 inthe pgi gene at locus ECD_03897), after optimal global alignment of both genomes; or- any combination thereof.

10. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in carbohydrate transport and / or carbohydrate metabolism is selected from the group consisting of: ygbM (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_02589), garK (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_02989), ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_00874), and any combination thereof; wherein the mutation is preferably located at a position, in the genome of the mutated bacterium, as defined below: -ygbM (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_02589): a position in the genome of the mutated bacterium equivalent to position2704598 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -garK (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_02989: a position in the genome of the mutated bacterium equivalent to position3137823 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -ybjT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locustag : ECD_00874) : a position in the genome of the mutated bacterium equivalent to position912803 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 184 inthe ybjT gene at locus ECD_00874), after optimal global alignment of both genomes;; or- any combination thereof.

11. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in lipid transport and / or lipid metabolism is cdsA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_00173),wherein the mutation is preferably located at a position in the genome of the mutated bacteriumequivalent to position 199016 in the genome of E. coli strain BL21(DE3), after optimal global alignmentof both genomes.

12. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in translation, ribosomal structure ribosomal biogenesis, and any combination thereof, is selected from the group consisting of: ligT (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_00146), rpsA (GenBank identification number forEscherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_00915) and any combination thereof;wherein the mutation is preferably located at a position, in the genome of the mutated bacterium, as defined below:- ligT (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_00146) : a position in the genome of the mutated bacterium equivalent to position164564 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -rpsA (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_00915): a position in the genome of the mutated bacterium equivalent to position968210 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; or -any combination thereof.

13. The mutated bacterium according to any one of the preceding claims, wherein the gene encodingproteins involved in transcription is selected from the group consisting of: ydcl (GenBankidentification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_01379), yfeR (GenBank identification number for Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_02308), ompR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_03257), basR (GenBank identification number for Escherichia coli strain BL21(DE3):CP001509.3, locus tag: ECD_03984), and any combination thereof;wherein the mutation is preferably located at a position, in the genome of the mutated bacterium, as defined below: -ydcl (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_01379) : a position in the genome of the mutated bacterium equivalent to position1449046 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -yfeR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_02308): a position in the genome of the mutated bacterium equivalent to position2399087 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -ompR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3,locus tag: ECD_03257: a position in the genome of the mutated bacterium equivalent toposition 3396345 in the genome of E. coli strain BL21(DE3) (corresponding to relative position620 in the ompR gene at locus ECD_03257), after optimal global alignment of both genomes;- basR (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03984): a position in the genome of the mutated bacterium equivalent to position4240680 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 350 inthe basR gene at locus ECD_03984), after optimal global alignment of both genomes; or- any combination thereof.

14. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in cell wall biogenesis, cell membrane biogenesis, cell envelope biogenesis, and any combination thereof, is selected from the group consisting of: ybjT (GenBank identification numberfor Escherichia coli strain BL21(DE3) : CP001509.3, locus tag : ECD_00874), etk (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag: ECD_00984), and any combination thereof; wherein the mutation is preferably located at a position, in the genome of the mutated bacterium, as defined below: -ybjT (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag : ECD_00874) : a position in the genome of the mutated bacterium equivalent to position912803 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; -etk (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00984): a position in the genome of the mutated bacterium equivalent to position1047795 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 1505 inthe etk gene at locus ECD_00984), after optimal global alignment of both genomes; or- any combination thereof.

15. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in intracellular trafficking, secretion, vesicular transport, and any combination thereof, is tcyP (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_01698),wherein the mutation is preferably located at a position in the genome of the mutated bacteriumequivalent to position 1755734 in the genome of E. coli strain BL21(DE3), after optimal globalalignment of both genomes.

16. The mutated bacterium according to any one of the preceding claims, wherein the gene encoding proteins involved in signal transduction mechanisms is pyrS (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locus tag : ECD_02290); wherein the mutation is preferably located at a position in the genome of the mutated bacteriumequivalent to position 2376813 in the genome of E. coli strain BL21(DE3), after optimal globalalignment of both genomes.

17. The mutated bacterium according to any one of the preceding claims, wherein the gene encodingproteins involved in inorganic ion transport and / or inorganic ion metabolism is selected from thegroup consisting of: cydD (GenBank identification number for Escherichia coli strain BL21(DE3):CP001509.3, locus tag : ECD_00891), dcuD (GenBank identification number for Escherichia coli strainBL21(DE3): CP001509.3, locus tag: ECD_03087), and any combination thereof;wherein the mutation is preferably located at a position, in the genome of the mutated bacterium,as defined below: -cydD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_00891): a position in the genome of the mutated bacterium equivalent to position934275 in the genome of E. coli strain BL21(DE3) (corresponding to relative position 1744 inthe cydD gene at locus ECD_00891), after optimal global alignment of both genomes;- dcuD (GenBank identification number for Escherichia coli strain BL21(DE3): CP001509.3, locustag: ECD_03087): a position in the genome of the mutated bacterium equivalent to position3236544 in the genome of E. coli strain BL21(DE3), after optimal global alignment of bothgenomes; or -any combination thereof.

18. The mutated bacterium according to any one of the preceding claims, wherein the mutated diderm bacterium is mutated in : -the gene yjgL (GenBank identification number for Escherichia coli strain BL21(DE3):CP001509.3, locus tag : ECD_04119), wherein the mutation is preferably located at a position in the genome of the mutated bacterium equivalent to position 4387431 in the genome of E. coli strain BL21(DE3), after optimal global alignment of both genomes; and / or -the gene yqjA (GenBank identification number for Escherichia coli strain BL21(DE3) :CP001509.3, locus tag : ECD_02964), wherein the mutation is preferably located at a position in the genome of the mutated bacterium equivalent to position 3114100 in the genome of E. coli strain BL21(DE3), after optimal global alignment of both genomes.

19. The mutated bacterium according to any one of the preceding claims, which may be obtained bya method comprising: a) growing a reference bacterium in continuous culture under turbidostat regime in a permissivemedium comprising a permissive concentration Cp of an amine compound equal to itsminimum inhibitory concentration (MIC) for the reference bacterium minus 10-20% (MIC-10-20%) for one to five days (preferably for three or four days); b) growing the bacterial population obtained at the end of step a), using:(i) turbidostat regime with gradual increase from Cp of the concentration of the aminecompound in the culture medium, until the bacterial population grows in a stressingmedium comprising a stressing concentration Cs of amine compound, wherein theCs is preferably about 1.2xCp, preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp; and / or (ii) medium swap regime using:^ a permissive medium comprising a permissive concentration of the aminecompound equal to Cp, and^ a stressing medium comprising a stressing concentration Cs of the aminecompound, wherein the Cs is preferably about 1.2xCp, preferably about 1.5xCp, more preferably about 2xCp, more preferably at least 2xCp, until the proportion of dilutions with the stressing medium reaches 100%;c) growing the bacterial population obtained at the end of step b) under turbidostat regime forone to 5 days (preferably for three days) in a medium comprising a concentration of the amine compound equal to Cs; d) selecting the best growing bacterial isolate; ande) optionally, repeating steps a) to d) using the best growing bacterial isolate as a new referencebacterium, except that: (iii) the same amine compound is used and the new Cp in repeated step a) is equal to Cs inthe previous step c), or (iv) another amine compound is used and Cp in repeated step a) is equal to the MIC of theother amine compound for the new reference bacterium minus 10-20%.

20. The mutated bacterium according to any one of the preceding claims, wherein the mutated bacterium is selected from the group consisting of: i. a mutated bacterium of the strain JHX 1.2.3, deposited under the provisions of Budapesttreaty, at the Collection Nationale de Cultures de Microorganismes (CNCM, having the address: CNCM, Institut Pasteur, 25 rue du Docteur Roux, F-75724 Paris Cedex 15), on 31January 2024, under the deposit number CNCM I-6031; and ii. a mutated bacterium of the strain JHX 4.2.8, deposited under the provisions of Budapesttreaty, at the Collection Nationale de Cultures de Microorganismes (CNCM, having the address: CNCM, Institut Pasteur, 25 rue du Docteur Roux, F-75724 Paris Cedex 15), on 31 January 2024, under the deposit number CNCM I-6032.

21. An in vitro use of the mutated bacterium according to any one claims 1 to 20, for thetransformation (preferably the biotransformation) of amine compounds, or for the production(preferably the bioproduction) of amine compounds, or any combination thereof;wherein the amine compound is preferably selected from the group consisting of a compound of formula(Formula I);wherein :a) R1 and R2 are independently selected from the groups H, alkyl, heteroalkyl, alkenyl, aryl,heteroaryl, arylalkyl, heteroaryl alkyl, aryl alkenyl, heteroaryl alkenyl, alkyloxy alkyl, heteroaryloxy alkyl, aryloxy alkyl, and alkanoyl alkyl, with proviso that R1 and R2 are notboth H, or b) R1 and R2 form together a saturated or non-saturated ring optionally fused with another ring,And wherein R3 is selected from the groups H, alkyl, alkenyl, alkynyl, and aryl.

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