The invention provides a non-naturally occurring microbial organism having an adipate, 6-aminocaproic acid or caprolactam pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective adipate, 6-aminocaproic acid or caprolactam pathway. The invention additionally provides a method for producing adipate, 6-aminocaproic acid or caprolactam. The method can include culturing an adipate, 6-aminocaproic acid or caprolactam producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding an adipate, 6-aminocaproic acid or caprolactam pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce adipate, 6-aminocaproic acid or caprolactam.

Provided are a novel 3-hydroxypropionate-lactate block copolymer [P(3HP-b-LA)], and a method for preparing same, comprising: a) transforming a recombinant microorganism modified to be incapable of biosynthesizing lactic acid with a vector including a 3-hydroxypropionyl-CoA biosynthesis gene and a polyhydroxyalkanoate (PHA) synthetase gene, and a vector including a lactate biosynthesis gene and a gene of an enzyme that converts lactate to lactyl-CoA; (b) synthesizing poly(3-hydroxypropionate) (P(3HP)) by culturing the recombinant microorganism using a glycerol as a carbon source; and (c) inhibiting P(3HP) production by adding IPTG and glucose, and biosynthesizing polylactate (PLA) at the end of P(3HP) synthesized in step (b) by enabling the expression of a lactate biosynthesis enzyme and an enzyme that converts lactate to lactyl-CoA. Also provided is a recombinant microorganism produced in step a).

The present disclosure provides methods for preparing β-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a β-substituted serine, and iii) a tryptophan synthase β-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the β-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new β-substituted tryptophan analogs are also described.

The invention is in the field of enzymology. More in particular, it provides a method for the isomerization of glucose into fructose wherein the glucose is derived from lignocellulosic material. More in particular, the invention provides polypeptides encoding mutant glucose isomerase enzymes with improved glucose isomerase activity as compared to the corresponding wild type enzyme. The disclosed polypeptides are particularly suited for converting glucose to fructose in the presence of xylose.

According to the present invention, theanine can efficiently be produced without exogenously adding ethylamine and without accumulation or leftover of ethylamine as a byproduct, by using a microorganism having enhanced activity to produce ethylamine with acetaldehyde and alanine as substrates and having enhanced activity of γ-glutamylmethylamide synthetase or glutaminase.

The invention provides microorganisms genetically modified to overexpress thermophilic lysine decarboxylase polypeptides in a mesophilic host to enhance the production of lysine and lysine derivatives by the microorganism, method of generating such microorganism, and methods of producing lysine and lysine derivatives using the genetically modified microorganisms.

The present invention relates to the field of genetic engineering, particularly to phytase variant YeAPPA having improved pepsin resistance and acid resistance, and increased catalytic efficiency, by substituting Leucine at the 162.sup.th site of the sequence set forth in SEQ ID NO.1 with glycine or proline or substituting glutamic acid at the 230.sup.th site of the sequence set forth in SEQ ID NO.1 with glycine, proline or arginine, in the benefit of the development of economical feed enzyme industry.

The disclosure relates to acetyl-CoA carboxylase (ACC) variants and host cells expressing them for the production of malonyl-CoA derived compounds including fatty acid derivatives. Further contemplated are methods of producing increased amounts of malonyl-CoA derived compounds and related cell cultures.

Provided are an O-succinyl homoserine transferase variant, a polynucleotide encoding the variant, a microorganism comprising the variant, and a method of producing O-succinyl homoserine using the microorganism.

The present invention relates to antimicrobial agents against Gram-positive bacteria, in particular to fusion proteins composed of an enzyme having the activity of degrading the cell wall of Gram-positive bacteria and an additional peptide stretch fused to the enzyme at the N- or C-terminus. Moreover, the present invention relates to nucleic acid molecules encoding said fusion protein, vectors comprising said nucleic acid molecules and host cells comprising either said nucleic acid molecules or said vectors. In addition, the present invention relates to said fusion protein for use as a medicament, in particular for the treatment or prevention of Gram-positive bacterial infections, as diagnostic means or as cosmetic substance. The present invention also relates to the treatment or prevention of Gram-positive bacterial contamination of foodstuff, of food processing equipment, of food processing plants, of surfaces coming into contact with foodstuff, of medical devices, of surfaces in hospitals and surgeries. Further, the present invention relates to a pharmaceutical composition comprising said fusion protein.